data_9H92
# 
_entry.id   9H92 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9H92         pdb_00009h92 10.2210/pdb9h92/pdb 
WWPDB D_1292142861 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-19 ? 
2 'Structure model' 1 1 2025-04-02 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H92 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gwen.tjallinks@iusspavia.it 
_pdbx_contact_author.name_first         Gwen 
_pdbx_contact_author.name_last          Tjallinks 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5174-913X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tjallinks, G.' 1 0000-0002-5174-913X 
'Mattevi, A.'   2 0000-0002-9523-7128 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Chem.Biol.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1554-8937 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            20 
_citation.language                  ? 
_citation.page_first                646 
_citation.page_last                 655 
_citation.title                     
;Structural and Mechanistic Characterization of the Flavin-Dependent Monooxygenase and Oxidase Involved in Sorbicillinoid Biosynthesis.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acschembio.4c00783 
_citation.pdbx_database_id_PubMed   40052414 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Tjallinks, G.'   1 ? 
primary 'Angeleri, N.'    2 ? 
primary 'Nguyen, Q.T.'    3 ? 
primary 'Mannucci, B.'    4 ? 
primary 'Arentshorst, M.' 5 ? 
primary 'Visser, J.'      6 ? 
primary 'Ram, A.F.J.'     7 ? 
primary 'Fraaije, M.W.'   8 ? 
primary 'Mattevi, A.'     9 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'FAD-linked oxidoreductase sorD' 50444.559 1   1.1.1.- ? ? ? 
2 branched    man 
;alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
748.682   1   ?       ? ? ? 
3 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   2   ?       
? ? ? 
4 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   1   ?       ? ? ? 
5 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   2   ?       ? ? ? 
6 non-polymer syn 'THIOCYANATE ION' 58.082    1   ?       ? ? ? 
7 water       nat water 18.015    604 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Sorbicillinoid biosynthetic cluster protein D' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MQAASAFATCLLASVGGNSSAVAFPNQANYSTLVAPYNFDLLTTPSAIVWPQDTQQVAAAVKCAVDSDIKVQPKSGGHNY
GNYGSTTGELSVNLDNLQHFSMNETSWTARLGPGNRLGRVTELMYNNGGRHVPHGTTFTVGLGGHATVGGAGAASRMHGL
LLDYVEEVEVVLANSSIVRASKSHNEDLFFAVRGAASSVGIVTDFSIRTEPVPVSSVTYSYIWEGTDPAARAEVFLTWQS
LLAGGSLPQHMAYDLVATANSMILGGAYFGSQEDFEAFNLSSHFKVAPDVTHIKTYTNFFDFSAAASAQTKAAGIASPSH
FYAKSLVFNQQTLIPDDAAEEVFKYLATTKNGTDLYAVTFAALGGAVRDVSASETAFYHRDASYFMFSFGRTSGDLTDTT
VQFLDGLSEVLTSGQPDAYYGQYVGNVDPRQPTDEALTGYYGKNLHRLQQIKSAVDPNDVFHNQQSIPPLS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MQAASAFATCLLASVGGNSSAVAFPNQANYSTLVAPYNFDLLTTPSAIVWPQDTQQVAAAVKCAVDSDIKVQPKSGGHNY
GNYGSTTGELSVNLDNLQHFSMNETSWTARLGPGNRLGRVTELMYNNGGRHVPHGTTFTVGLGGHATVGGAGAASRMHGL
LLDYVEEVEVVLANSSIVRASKSHNEDLFFAVRGAASSVGIVTDFSIRTEPVPVSSVTYSYIWEGTDPAARAEVFLTWQS
LLAGGSLPQHMAYDLVATANSMILGGAYFGSQEDFEAFNLSSHFKVAPDVTHIKTYTNFFDFSAAASAQTKAAGIASPSH
FYAKSLVFNQQTLIPDDAAEEVFKYLATTKNGTDLYAVTFAALGGAVRDVSASETAFYHRDASYFMFSFGRTSGDLTDTT
VQFLDGLSEVLTSGQPDAYYGQYVGNVDPRQPTDEALTGYYGKNLHRLQQIKSAVDPNDVFHNQQSIPPLS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'FLAVIN-ADENINE DINUCLEOTIDE'            FAD 
5 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
6 'THIOCYANATE ION'                        SCN 
7 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLN n 
1 3   ALA n 
1 4   ALA n 
1 5   SER n 
1 6   ALA n 
1 7   PHE n 
1 8   ALA n 
1 9   THR n 
1 10  CYS n 
1 11  LEU n 
1 12  LEU n 
1 13  ALA n 
1 14  SER n 
1 15  VAL n 
1 16  GLY n 
1 17  GLY n 
1 18  ASN n 
1 19  SER n 
1 20  SER n 
1 21  ALA n 
1 22  VAL n 
1 23  ALA n 
1 24  PHE n 
1 25  PRO n 
1 26  ASN n 
1 27  GLN n 
1 28  ALA n 
1 29  ASN n 
1 30  TYR n 
1 31  SER n 
1 32  THR n 
1 33  LEU n 
1 34  VAL n 
1 35  ALA n 
1 36  PRO n 
1 37  TYR n 
1 38  ASN n 
1 39  PHE n 
1 40  ASP n 
1 41  LEU n 
1 42  LEU n 
1 43  THR n 
1 44  THR n 
1 45  PRO n 
1 46  SER n 
1 47  ALA n 
1 48  ILE n 
1 49  VAL n 
1 50  TRP n 
1 51  PRO n 
1 52  GLN n 
1 53  ASP n 
1 54  THR n 
1 55  GLN n 
1 56  GLN n 
1 57  VAL n 
1 58  ALA n 
1 59  ALA n 
1 60  ALA n 
1 61  VAL n 
1 62  LYS n 
1 63  CYS n 
1 64  ALA n 
1 65  VAL n 
1 66  ASP n 
1 67  SER n 
1 68  ASP n 
1 69  ILE n 
1 70  LYS n 
1 71  VAL n 
1 72  GLN n 
1 73  PRO n 
1 74  LYS n 
1 75  SER n 
1 76  GLY n 
1 77  GLY n 
1 78  HIS n 
1 79  ASN n 
1 80  TYR n 
1 81  GLY n 
1 82  ASN n 
1 83  TYR n 
1 84  GLY n 
1 85  SER n 
1 86  THR n 
1 87  THR n 
1 88  GLY n 
1 89  GLU n 
1 90  LEU n 
1 91  SER n 
1 92  VAL n 
1 93  ASN n 
1 94  LEU n 
1 95  ASP n 
1 96  ASN n 
1 97  LEU n 
1 98  GLN n 
1 99  HIS n 
1 100 PHE n 
1 101 SER n 
1 102 MET n 
1 103 ASN n 
1 104 GLU n 
1 105 THR n 
1 106 SER n 
1 107 TRP n 
1 108 THR n 
1 109 ALA n 
1 110 ARG n 
1 111 LEU n 
1 112 GLY n 
1 113 PRO n 
1 114 GLY n 
1 115 ASN n 
1 116 ARG n 
1 117 LEU n 
1 118 GLY n 
1 119 ARG n 
1 120 VAL n 
1 121 THR n 
1 122 GLU n 
1 123 LEU n 
1 124 MET n 
1 125 TYR n 
1 126 ASN n 
1 127 ASN n 
1 128 GLY n 
1 129 GLY n 
1 130 ARG n 
1 131 HIS n 
1 132 VAL n 
1 133 PRO n 
1 134 HIS n 
1 135 GLY n 
1 136 THR n 
1 137 THR n 
1 138 PHE n 
1 139 THR n 
1 140 VAL n 
1 141 GLY n 
1 142 LEU n 
1 143 GLY n 
1 144 GLY n 
1 145 HIS n 
1 146 ALA n 
1 147 THR n 
1 148 VAL n 
1 149 GLY n 
1 150 GLY n 
1 151 ALA n 
1 152 GLY n 
1 153 ALA n 
1 154 ALA n 
1 155 SER n 
1 156 ARG n 
1 157 MET n 
1 158 HIS n 
1 159 GLY n 
1 160 LEU n 
1 161 LEU n 
1 162 LEU n 
1 163 ASP n 
1 164 TYR n 
1 165 VAL n 
1 166 GLU n 
1 167 GLU n 
1 168 VAL n 
1 169 GLU n 
1 170 VAL n 
1 171 VAL n 
1 172 LEU n 
1 173 ALA n 
1 174 ASN n 
1 175 SER n 
1 176 SER n 
1 177 ILE n 
1 178 VAL n 
1 179 ARG n 
1 180 ALA n 
1 181 SER n 
1 182 LYS n 
1 183 SER n 
1 184 HIS n 
1 185 ASN n 
1 186 GLU n 
1 187 ASP n 
1 188 LEU n 
1 189 PHE n 
1 190 PHE n 
1 191 ALA n 
1 192 VAL n 
1 193 ARG n 
1 194 GLY n 
1 195 ALA n 
1 196 ALA n 
1 197 SER n 
1 198 SER n 
1 199 VAL n 
1 200 GLY n 
1 201 ILE n 
1 202 VAL n 
1 203 THR n 
1 204 ASP n 
1 205 PHE n 
1 206 SER n 
1 207 ILE n 
1 208 ARG n 
1 209 THR n 
1 210 GLU n 
1 211 PRO n 
1 212 VAL n 
1 213 PRO n 
1 214 VAL n 
1 215 SER n 
1 216 SER n 
1 217 VAL n 
1 218 THR n 
1 219 TYR n 
1 220 SER n 
1 221 TYR n 
1 222 ILE n 
1 223 TRP n 
1 224 GLU n 
1 225 GLY n 
1 226 THR n 
1 227 ASP n 
1 228 PRO n 
1 229 ALA n 
1 230 ALA n 
1 231 ARG n 
1 232 ALA n 
1 233 GLU n 
1 234 VAL n 
1 235 PHE n 
1 236 LEU n 
1 237 THR n 
1 238 TRP n 
1 239 GLN n 
1 240 SER n 
1 241 LEU n 
1 242 LEU n 
1 243 ALA n 
1 244 GLY n 
1 245 GLY n 
1 246 SER n 
1 247 LEU n 
1 248 PRO n 
1 249 GLN n 
1 250 HIS n 
1 251 MET n 
1 252 ALA n 
1 253 TYR n 
1 254 ASP n 
1 255 LEU n 
1 256 VAL n 
1 257 ALA n 
1 258 THR n 
1 259 ALA n 
1 260 ASN n 
1 261 SER n 
1 262 MET n 
1 263 ILE n 
1 264 LEU n 
1 265 GLY n 
1 266 GLY n 
1 267 ALA n 
1 268 TYR n 
1 269 PHE n 
1 270 GLY n 
1 271 SER n 
1 272 GLN n 
1 273 GLU n 
1 274 ASP n 
1 275 PHE n 
1 276 GLU n 
1 277 ALA n 
1 278 PHE n 
1 279 ASN n 
1 280 LEU n 
1 281 SER n 
1 282 SER n 
1 283 HIS n 
1 284 PHE n 
1 285 LYS n 
1 286 VAL n 
1 287 ALA n 
1 288 PRO n 
1 289 ASP n 
1 290 VAL n 
1 291 THR n 
1 292 HIS n 
1 293 ILE n 
1 294 LYS n 
1 295 THR n 
1 296 TYR n 
1 297 THR n 
1 298 ASN n 
1 299 PHE n 
1 300 PHE n 
1 301 ASP n 
1 302 PHE n 
1 303 SER n 
1 304 ALA n 
1 305 ALA n 
1 306 ALA n 
1 307 SER n 
1 308 ALA n 
1 309 GLN n 
1 310 THR n 
1 311 LYS n 
1 312 ALA n 
1 313 ALA n 
1 314 GLY n 
1 315 ILE n 
1 316 ALA n 
1 317 SER n 
1 318 PRO n 
1 319 SER n 
1 320 HIS n 
1 321 PHE n 
1 322 TYR n 
1 323 ALA n 
1 324 LYS n 
1 325 SER n 
1 326 LEU n 
1 327 VAL n 
1 328 PHE n 
1 329 ASN n 
1 330 GLN n 
1 331 GLN n 
1 332 THR n 
1 333 LEU n 
1 334 ILE n 
1 335 PRO n 
1 336 ASP n 
1 337 ASP n 
1 338 ALA n 
1 339 ALA n 
1 340 GLU n 
1 341 GLU n 
1 342 VAL n 
1 343 PHE n 
1 344 LYS n 
1 345 TYR n 
1 346 LEU n 
1 347 ALA n 
1 348 THR n 
1 349 THR n 
1 350 LYS n 
1 351 ASN n 
1 352 GLY n 
1 353 THR n 
1 354 ASP n 
1 355 LEU n 
1 356 TYR n 
1 357 ALA n 
1 358 VAL n 
1 359 THR n 
1 360 PHE n 
1 361 ALA n 
1 362 ALA n 
1 363 LEU n 
1 364 GLY n 
1 365 GLY n 
1 366 ALA n 
1 367 VAL n 
1 368 ARG n 
1 369 ASP n 
1 370 VAL n 
1 371 SER n 
1 372 ALA n 
1 373 SER n 
1 374 GLU n 
1 375 THR n 
1 376 ALA n 
1 377 PHE n 
1 378 TYR n 
1 379 HIS n 
1 380 ARG n 
1 381 ASP n 
1 382 ALA n 
1 383 SER n 
1 384 TYR n 
1 385 PHE n 
1 386 MET n 
1 387 PHE n 
1 388 SER n 
1 389 PHE n 
1 390 GLY n 
1 391 ARG n 
1 392 THR n 
1 393 SER n 
1 394 GLY n 
1 395 ASP n 
1 396 LEU n 
1 397 THR n 
1 398 ASP n 
1 399 THR n 
1 400 THR n 
1 401 VAL n 
1 402 GLN n 
1 403 PHE n 
1 404 LEU n 
1 405 ASP n 
1 406 GLY n 
1 407 LEU n 
1 408 SER n 
1 409 GLU n 
1 410 VAL n 
1 411 LEU n 
1 412 THR n 
1 413 SER n 
1 414 GLY n 
1 415 GLN n 
1 416 PRO n 
1 417 ASP n 
1 418 ALA n 
1 419 TYR n 
1 420 TYR n 
1 421 GLY n 
1 422 GLN n 
1 423 TYR n 
1 424 VAL n 
1 425 GLY n 
1 426 ASN n 
1 427 VAL n 
1 428 ASP n 
1 429 PRO n 
1 430 ARG n 
1 431 GLN n 
1 432 PRO n 
1 433 THR n 
1 434 ASP n 
1 435 GLU n 
1 436 ALA n 
1 437 LEU n 
1 438 THR n 
1 439 GLY n 
1 440 TYR n 
1 441 TYR n 
1 442 GLY n 
1 443 LYS n 
1 444 ASN n 
1 445 LEU n 
1 446 HIS n 
1 447 ARG n 
1 448 LEU n 
1 449 GLN n 
1 450 GLN n 
1 451 ILE n 
1 452 LYS n 
1 453 SER n 
1 454 ALA n 
1 455 VAL n 
1 456 ASP n 
1 457 PRO n 
1 458 ASN n 
1 459 ASP n 
1 460 VAL n 
1 461 PHE n 
1 462 HIS n 
1 463 ASN n 
1 464 GLN n 
1 465 GLN n 
1 466 SER n 
1 467 ILE n 
1 468 PRO n 
1 469 PRO n 
1 470 LEU n 
1 471 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   471 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'sorD, Pc21g05110' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Penicillium rubens Wisconsin 54-1255' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     500485 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Aspergillus niger' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     5061 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
3 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DManpa1-6DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                          'Glycam Condensed Sequence' GMML       
1.0   
2 2 'WURCS=2.0/2,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2-2/a4-b1_b4-c1_c6-d1'  WURCS                       PDB2Glycan 
1.1.0 
3 2 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{[(6+1)][a-D-Manp]{}}}}' LINUCS                      PDB-CARE   ? 
4 3 DGlcpNAcb1-4DGlcpNAcb1-ROH                                                            'Glycam Condensed Sequence' GMML       
1.0   
5 3 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                                 WURCS                       PDB2Glycan 
1.1.0 
6 3 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'                                       LINUCS                      PDB-CARE   ? 
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 2 3 MAN C1 O1 2 NAG O4 HO4 sing ? 
3 2 4 MAN C1 O1 3 MAN O6 HO6 sing ? 
4 3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'           y ALANINE                                  ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking'           y ARGININE                                 ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking'           y ASPARAGINE                               ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking'           y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking'           y CYSTEINE                                 ? 'C3 H7 N O2 S'      121.158 
FAD non-polymer                   . 'FLAVIN-ADENINE DINUCLEOTIDE'            ? 'C27 H33 N9 O15 P2' 785.550 
GLN 'L-peptide linking'           y GLUTAMINE                                ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking'           y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'             y GLYCINE                                  ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking'           y HISTIDINE                                ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer                   . WATER                                    ? 'H2 O'              18.015  
ILE 'L-peptide linking'           y ISOLEUCINE                               ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking'           y LEUCINE                                  ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking'           y LYSINE                                   ? 'C6 H15 N2 O2 1'    147.195 
MAN 'D-saccharide, alpha linking' . alpha-D-mannopyranose                    'alpha-D-mannose; D-mannose; mannose' 'C6 H12 O6' 
180.156 
MET 'L-peptide linking'           y METHIONINE                               ? 'C5 H11 N O2 S'     149.211 
NAG 'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'       221.208 
PHE 'L-peptide linking'           y PHENYLALANINE                            ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking'           y PROLINE                                  ? 'C5 H9 N O2'        115.130 
SCN non-polymer                   . 'THIOCYANATE ION'                        ? 'C N S -1'          58.082  
SER 'L-peptide linking'           y SERINE                                   ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking'           y THREONINE                                ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN                               ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking'           y TYROSINE                                 ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking'           y VALINE                                   ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLN 2   2   ?   ?   ?   A . n 
A 1 3   ALA 3   3   ?   ?   ?   A . n 
A 1 4   ALA 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   ALA 8   8   8   ALA ALA A . n 
A 1 9   THR 9   9   9   THR THR A . n 
A 1 10  CYS 10  10  10  CYS CYS A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  SER 20  20  20  SER SER A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  VAL 22  22  22  VAL VAL A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  ASN 29  29  29  ASN ASN A . n 
A 1 30  TYR 30  30  30  TYR TYR A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  ASN 38  38  38  ASN ASN A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  ILE 48  48  48  ILE ILE A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  TRP 50  50  50  TRP TRP A . n 
A 1 51  PRO 51  51  51  PRO PRO A . n 
A 1 52  GLN 52  52  52  GLN GLN A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  GLN 56  56  56  GLN GLN A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  CYS 63  63  63  CYS CYS A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  GLN 72  72  72  GLN GLN A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  LYS 74  74  74  LYS LYS A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  HIS 78  78  78  HIS HIS A . n 
A 1 79  ASN 79  79  79  ASN ASN A . n 
A 1 80  TYR 80  80  80  TYR TYR A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  ASN 82  82  82  ASN ASN A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  ASN 93  93  93  ASN ASN A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  GLN 98  98  98  GLN GLN A . n 
A 1 99  HIS 99  99  99  HIS HIS A . n 
A 1 100 PHE 100 100 100 PHE PHE A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 MET 102 102 102 MET MET A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 TRP 107 107 107 TRP TRP A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 ARG 110 110 110 ARG ARG A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 MET 124 124 124 MET MET A . n 
A 1 125 TYR 125 125 125 TYR TYR A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 ARG 130 130 130 ARG ARG A . n 
A 1 131 HIS 131 131 131 HIS HIS A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 HIS 134 134 134 HIS HIS A . n 
A 1 135 GLY 135 135 135 GLY GLY A . n 
A 1 136 THR 136 136 136 THR THR A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 VAL 140 140 140 VAL VAL A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 HIS 145 145 145 HIS HIS A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 MET 157 157 157 MET MET A . n 
A 1 158 HIS 158 158 158 HIS HIS A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 ASP 163 163 163 ASP ASP A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 GLU 169 169 169 GLU GLU A . n 
A 1 170 VAL 170 170 170 VAL VAL A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 ASN 174 174 174 ASN ASN A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 LYS 182 182 182 LYS LYS A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 HIS 184 184 184 HIS HIS A . n 
A 1 185 ASN 185 185 185 ASN ASN A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 PHE 190 190 190 PHE PHE A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 GLY 200 200 200 GLY GLY A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 ASP 204 204 204 ASP ASP A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 ILE 207 207 207 ILE ILE A . n 
A 1 208 ARG 208 208 208 ARG ARG A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 PRO 213 213 213 PRO PRO A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 TYR 219 219 219 TYR TYR A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 TYR 221 221 221 TYR TYR A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 TRP 223 223 223 TRP TRP A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 ASP 227 227 227 ASP ASP A . n 
A 1 228 PRO 228 228 228 PRO PRO A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 ARG 231 231 231 ARG ARG A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 THR 237 237 237 THR THR A . n 
A 1 238 TRP 238 238 238 TRP TRP A . n 
A 1 239 GLN 239 239 239 GLN GLN A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 GLY 244 244 244 GLY GLY A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 LEU 247 247 247 LEU LEU A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 GLN 249 249 249 GLN GLN A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 MET 251 251 251 MET MET A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 TYR 253 253 253 TYR TYR A . n 
A 1 254 ASP 254 254 254 ASP ASP A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 THR 258 258 258 THR THR A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 ASN 260 260 260 ASN ASN A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 MET 262 262 262 MET MET A . n 
A 1 263 ILE 263 263 263 ILE ILE A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 ALA 267 267 267 ALA ALA A . n 
A 1 268 TYR 268 268 268 TYR TYR A . n 
A 1 269 PHE 269 269 269 PHE PHE A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 GLN 272 272 272 GLN GLN A . n 
A 1 273 GLU 273 273 273 GLU GLU A . n 
A 1 274 ASP 274 274 274 ASP ASP A . n 
A 1 275 PHE 275 275 275 PHE PHE A . n 
A 1 276 GLU 276 276 276 GLU GLU A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 PHE 278 278 278 PHE PHE A . n 
A 1 279 ASN 279 279 279 ASN ASN A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 SER 281 281 281 SER SER A . n 
A 1 282 SER 282 282 282 SER SER A . n 
A 1 283 HIS 283 283 283 HIS HIS A . n 
A 1 284 PHE 284 284 284 PHE PHE A . n 
A 1 285 LYS 285 285 285 LYS LYS A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 VAL 290 290 290 VAL VAL A . n 
A 1 291 THR 291 291 291 THR ALA A . n 
A 1 292 HIS 292 292 292 HIS HIS A . n 
A 1 293 ILE 293 293 293 ILE ILE A . n 
A 1 294 LYS 294 294 294 LYS LYS A . n 
A 1 295 THR 295 295 295 THR THR A . n 
A 1 296 TYR 296 296 296 TYR TYR A . n 
A 1 297 THR 297 297 297 THR THR A . n 
A 1 298 ASN 298 298 298 ASN ASN A . n 
A 1 299 PHE 299 299 299 PHE PHE A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 ASP 301 301 301 ASP ASP A . n 
A 1 302 PHE 302 302 302 PHE PHE A . n 
A 1 303 SER 303 303 303 SER SER A . n 
A 1 304 ALA 304 304 304 ALA ALA A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 GLN 309 309 309 GLN GLN A . n 
A 1 310 THR 310 310 310 THR THR A . n 
A 1 311 LYS 311 311 311 LYS LYS A . n 
A 1 312 ALA 312 312 312 ALA ALA A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 GLY 314 314 314 GLY GLY A . n 
A 1 315 ILE 315 315 315 ILE ILE A . n 
A 1 316 ALA 316 316 316 ALA ALA A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 PRO 318 318 318 PRO PRO A . n 
A 1 319 SER 319 319 319 SER SER A . n 
A 1 320 HIS 320 320 320 HIS HIS A . n 
A 1 321 PHE 321 321 321 PHE PHE A . n 
A 1 322 TYR 322 322 322 TYR TYR A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 LYS 324 324 324 LYS LYS A . n 
A 1 325 SER 325 325 325 SER SER A . n 
A 1 326 LEU 326 326 326 LEU LEU A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 PHE 328 328 328 PHE PHE A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 GLN 330 330 330 GLN GLN A . n 
A 1 331 GLN 331 331 331 GLN GLN A . n 
A 1 332 THR 332 332 332 THR THR A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 ILE 334 334 334 ILE ILE A . n 
A 1 335 PRO 335 335 335 PRO PRO A . n 
A 1 336 ASP 336 336 336 ASP ASP A . n 
A 1 337 ASP 337 337 337 ASP ASP A . n 
A 1 338 ALA 338 338 338 ALA ALA A . n 
A 1 339 ALA 339 339 339 ALA ALA A . n 
A 1 340 GLU 340 340 340 GLU GLU A . n 
A 1 341 GLU 341 341 341 GLU GLU A . n 
A 1 342 VAL 342 342 342 VAL VAL A . n 
A 1 343 PHE 343 343 343 PHE PHE A . n 
A 1 344 LYS 344 344 344 LYS LYS A . n 
A 1 345 TYR 345 345 345 TYR TYR A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 THR 348 348 348 THR THR A . n 
A 1 349 THR 349 349 349 THR THR A . n 
A 1 350 LYS 350 350 350 LYS LYS A . n 
A 1 351 ASN 351 351 351 ASN ASN A . n 
A 1 352 GLY 352 352 352 GLY GLY A . n 
A 1 353 THR 353 353 353 THR THR A . n 
A 1 354 ASP 354 354 354 ASP ASP A . n 
A 1 355 LEU 355 355 355 LEU LEU A . n 
A 1 356 TYR 356 356 356 TYR TYR A . n 
A 1 357 ALA 357 357 357 ALA ALA A . n 
A 1 358 VAL 358 358 358 VAL VAL A . n 
A 1 359 THR 359 359 359 THR THR A . n 
A 1 360 PHE 360 360 360 PHE PHE A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 ALA 362 362 362 ALA ALA A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 GLY 365 365 365 GLY GLY A . n 
A 1 366 ALA 366 366 366 ALA ALA A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 ARG 368 368 368 ARG ARG A . n 
A 1 369 ASP 369 369 369 ASP ASP A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 SER 371 371 371 SER SER A . n 
A 1 372 ALA 372 372 372 ALA ALA A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 GLU 374 374 374 GLU GLU A . n 
A 1 375 THR 375 375 375 THR THR A . n 
A 1 376 ALA 376 376 376 ALA ALA A . n 
A 1 377 PHE 377 377 377 PHE PHE A . n 
A 1 378 TYR 378 378 378 TYR TYR A . n 
A 1 379 HIS 379 379 379 HIS HIS A . n 
A 1 380 ARG 380 380 380 ARG ARG A . n 
A 1 381 ASP 381 381 381 ASP ASP A . n 
A 1 382 ALA 382 382 382 ALA ALA A . n 
A 1 383 SER 383 383 383 SER SER A . n 
A 1 384 TYR 384 384 384 TYR TYR A . n 
A 1 385 PHE 385 385 385 PHE PHE A . n 
A 1 386 MET 386 386 386 MET MET A . n 
A 1 387 PHE 387 387 387 PHE PHE A . n 
A 1 388 SER 388 388 388 SER SER A . n 
A 1 389 PHE 389 389 389 PHE PHE A . n 
A 1 390 GLY 390 390 390 GLY GLY A . n 
A 1 391 ARG 391 391 391 ARG ARG A . n 
A 1 392 THR 392 392 392 THR THR A . n 
A 1 393 SER 393 393 393 SER SER A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 ASP 395 395 395 ASP ASP A . n 
A 1 396 LEU 396 396 396 LEU LEU A . n 
A 1 397 THR 397 397 397 THR THR A . n 
A 1 398 ASP 398 398 398 ASP ASP A . n 
A 1 399 THR 399 399 399 THR THR A . n 
A 1 400 THR 400 400 400 THR THR A . n 
A 1 401 VAL 401 401 401 VAL VAL A . n 
A 1 402 GLN 402 402 402 GLN GLN A . n 
A 1 403 PHE 403 403 403 PHE PHE A . n 
A 1 404 LEU 404 404 404 LEU LEU A . n 
A 1 405 ASP 405 405 405 ASP ASP A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 LEU 407 407 407 LEU LEU A . n 
A 1 408 SER 408 408 408 SER SER A . n 
A 1 409 GLU 409 409 409 GLU GLU A . n 
A 1 410 VAL 410 410 410 VAL VAL A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 THR 412 412 412 THR THR A . n 
A 1 413 SER 413 413 413 SER SER A . n 
A 1 414 GLY 414 414 414 GLY GLY A . n 
A 1 415 GLN 415 415 415 GLN GLN A . n 
A 1 416 PRO 416 416 416 PRO PRO A . n 
A 1 417 ASP 417 417 417 ASP ASP A . n 
A 1 418 ALA 418 418 418 ALA ALA A . n 
A 1 419 TYR 419 419 419 TYR TYR A . n 
A 1 420 TYR 420 420 420 TYR TYR A . n 
A 1 421 GLY 421 421 421 GLY GLY A . n 
A 1 422 GLN 422 422 422 GLN GLN A . n 
A 1 423 TYR 423 423 423 TYR TYR A . n 
A 1 424 VAL 424 424 424 VAL VAL A . n 
A 1 425 GLY 425 425 425 GLY GLY A . n 
A 1 426 ASN 426 426 426 ASN ASN A . n 
A 1 427 VAL 427 427 427 VAL VAL A . n 
A 1 428 ASP 428 428 428 ASP ASP A . n 
A 1 429 PRO 429 429 429 PRO PRO A . n 
A 1 430 ARG 430 430 430 ARG ARG A . n 
A 1 431 GLN 431 431 431 GLN GLN A . n 
A 1 432 PRO 432 432 432 PRO PRO A . n 
A 1 433 THR 433 433 433 THR THR A . n 
A 1 434 ASP 434 434 434 ASP ASP A . n 
A 1 435 GLU 435 435 435 GLU GLU A . n 
A 1 436 ALA 436 436 436 ALA ALA A . n 
A 1 437 LEU 437 437 437 LEU LEU A . n 
A 1 438 THR 438 438 438 THR THR A . n 
A 1 439 GLY 439 439 439 GLY GLY A . n 
A 1 440 TYR 440 440 440 TYR TYR A . n 
A 1 441 TYR 441 441 441 TYR TYR A . n 
A 1 442 GLY 442 442 442 GLY GLY A . n 
A 1 443 LYS 443 443 443 LYS LYS A . n 
A 1 444 ASN 444 444 444 ASN ASN A . n 
A 1 445 LEU 445 445 445 LEU LEU A . n 
A 1 446 HIS 446 446 446 HIS HIS A . n 
A 1 447 ARG 447 447 447 ARG ARG A . n 
A 1 448 LEU 448 448 448 LEU LEU A . n 
A 1 449 GLN 449 449 449 GLN GLN A . n 
A 1 450 GLN 450 450 450 GLN GLN A . n 
A 1 451 ILE 451 451 451 ILE ILE A . n 
A 1 452 LYS 452 452 452 LYS LYS A . n 
A 1 453 SER 453 453 453 SER SER A . n 
A 1 454 ALA 454 454 454 ALA ALA A . n 
A 1 455 VAL 455 455 455 VAL VAL A . n 
A 1 456 ASP 456 456 456 ASP ASP A . n 
A 1 457 PRO 457 457 457 PRO PRO A . n 
A 1 458 ASN 458 458 458 ASN ASN A . n 
A 1 459 ASP 459 459 459 ASP ASP A . n 
A 1 460 VAL 460 460 460 VAL VAL A . n 
A 1 461 PHE 461 461 461 PHE PHE A . n 
A 1 462 HIS 462 462 462 HIS HIS A . n 
A 1 463 ASN 463 463 463 ASN ASN A . n 
A 1 464 GLN 464 464 464 GLN GLN A . n 
A 1 465 GLN 465 465 465 GLN GLN A . n 
A 1 466 SER 466 466 466 SER SER A . n 
A 1 467 ILE 467 467 467 ILE ILE A . n 
A 1 468 PRO 468 468 468 PRO PRO A . n 
A 1 469 PRO 469 469 469 PRO PRO A . n 
A 1 470 LEU 470 470 470 LEU LEU A . n 
A 1 471 SER 471 471 ?   ?   ?   A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
B 2 NAG 1 B NAG 1 B NAG 1 n 
B 2 NAG 2 B NAG 2 B NAG 2 n 
B 2 MAN 3 B MAN 3 B MAN 3 n 
B 2 MAN 4 B MAN 4 B MAN 4 n 
C 3 NAG 1 C NAG 1 C NAG 1 n 
C 3 NAG 2 C NAG 2 C NAG 2 n 
D 3 NAG 1 D NAG 1 D NAG 1 n 
D 3 NAG 2 D NAG 2 D NAG 2 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FAD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 4 FAD 1   501  472 FAD FAD A . 
F 5 NAG 1   502  477 NAG NAG A . 
G 5 NAG 1   503  478 NAG NAG A . 
H 6 SCN 1   504  483 SCN SCN A . 
I 7 HOH 1   601  920 HOH HOH A . 
I 7 HOH 2   602  667 HOH HOH A . 
I 7 HOH 3   603  912 HOH HOH A . 
I 7 HOH 4   604  879 HOH HOH A . 
I 7 HOH 5   605  157 HOH HOH A . 
I 7 HOH 6   606  860 HOH HOH A . 
I 7 HOH 7   607  883 HOH HOH A . 
I 7 HOH 8   608  279 HOH HOH A . 
I 7 HOH 9   609  882 HOH HOH A . 
I 7 HOH 10  610  870 HOH HOH A . 
I 7 HOH 11  611  531 HOH HOH A . 
I 7 HOH 12  612  533 HOH HOH A . 
I 7 HOH 13  613  918 HOH HOH A . 
I 7 HOH 14  614  280 HOH HOH A . 
I 7 HOH 15  615  378 HOH HOH A . 
I 7 HOH 16  616  897 HOH HOH A . 
I 7 HOH 17  617  297 HOH HOH A . 
I 7 HOH 18  618  363 HOH HOH A . 
I 7 HOH 19  619  133 HOH HOH A . 
I 7 HOH 20  620  443 HOH HOH A . 
I 7 HOH 21  621  26  HOH HOH A . 
I 7 HOH 22  622  235 HOH HOH A . 
I 7 HOH 23  623  340 HOH HOH A . 
I 7 HOH 24  624  508 HOH HOH A . 
I 7 HOH 25  625  209 HOH HOH A . 
I 7 HOH 26  626  317 HOH HOH A . 
I 7 HOH 27  627  924 HOH HOH A . 
I 7 HOH 28  628  319 HOH HOH A . 
I 7 HOH 29  629  82  HOH HOH A . 
I 7 HOH 30  630  128 HOH HOH A . 
I 7 HOH 31  631  174 HOH HOH A . 
I 7 HOH 32  632  388 HOH HOH A . 
I 7 HOH 33  633  365 HOH HOH A . 
I 7 HOH 34  634  896 HOH HOH A . 
I 7 HOH 35  635  176 HOH HOH A . 
I 7 HOH 36  636  255 HOH HOH A . 
I 7 HOH 37  637  509 HOH HOH A . 
I 7 HOH 38  638  118 HOH HOH A . 
I 7 HOH 39  639  546 HOH HOH A . 
I 7 HOH 40  640  397 HOH HOH A . 
I 7 HOH 41  641  330 HOH HOH A . 
I 7 HOH 42  642  232 HOH HOH A . 
I 7 HOH 43  643  391 HOH HOH A . 
I 7 HOH 44  644  644 HOH HOH A . 
I 7 HOH 45  645  338 HOH HOH A . 
I 7 HOH 46  646  137 HOH HOH A . 
I 7 HOH 47  647  80  HOH HOH A . 
I 7 HOH 48  648  371 HOH HOH A . 
I 7 HOH 49  649  324 HOH HOH A . 
I 7 HOH 50  650  142 HOH HOH A . 
I 7 HOH 51  651  369 HOH HOH A . 
I 7 HOH 52  652  215 HOH HOH A . 
I 7 HOH 53  653  200 HOH HOH A . 
I 7 HOH 54  654  398 HOH HOH A . 
I 7 HOH 55  655  195 HOH HOH A . 
I 7 HOH 56  656  419 HOH HOH A . 
I 7 HOH 57  657  210 HOH HOH A . 
I 7 HOH 58  658  495 HOH HOH A . 
I 7 HOH 59  659  73  HOH HOH A . 
I 7 HOH 60  660  42  HOH HOH A . 
I 7 HOH 61  661  374 HOH HOH A . 
I 7 HOH 62  662  150 HOH HOH A . 
I 7 HOH 63  663  148 HOH HOH A . 
I 7 HOH 64  664  552 HOH HOH A . 
I 7 HOH 65  665  303 HOH HOH A . 
I 7 HOH 66  666  563 HOH HOH A . 
I 7 HOH 67  667  206 HOH HOH A . 
I 7 HOH 68  668  50  HOH HOH A . 
I 7 HOH 69  669  230 HOH HOH A . 
I 7 HOH 70  670  467 HOH HOH A . 
I 7 HOH 71  671  477 HOH HOH A . 
I 7 HOH 72  672  168 HOH HOH A . 
I 7 HOH 73  673  115 HOH HOH A . 
I 7 HOH 74  674  250 HOH HOH A . 
I 7 HOH 75  675  691 HOH HOH A . 
I 7 HOH 76  676  208 HOH HOH A . 
I 7 HOH 77  677  48  HOH HOH A . 
I 7 HOH 78  678  198 HOH HOH A . 
I 7 HOH 79  679  310 HOH HOH A . 
I 7 HOH 80  680  205 HOH HOH A . 
I 7 HOH 81  681  934 HOH HOH A . 
I 7 HOH 82  682  930 HOH HOH A . 
I 7 HOH 83  683  1   HOH HOH A . 
I 7 HOH 84  684  204 HOH HOH A . 
I 7 HOH 85  685  39  HOH HOH A . 
I 7 HOH 86  686  576 HOH HOH A . 
I 7 HOH 87  687  89  HOH HOH A . 
I 7 HOH 88  688  49  HOH HOH A . 
I 7 HOH 89  689  454 HOH HOH A . 
I 7 HOH 90  690  430 HOH HOH A . 
I 7 HOH 91  691  114 HOH HOH A . 
I 7 HOH 92  692  154 HOH HOH A . 
I 7 HOH 93  693  428 HOH HOH A . 
I 7 HOH 94  694  916 HOH HOH A . 
I 7 HOH 95  695  46  HOH HOH A . 
I 7 HOH 96  696  263 HOH HOH A . 
I 7 HOH 97  697  295 HOH HOH A . 
I 7 HOH 98  698  580 HOH HOH A . 
I 7 HOH 99  699  99  HOH HOH A . 
I 7 HOH 100 700  253 HOH HOH A . 
I 7 HOH 101 701  4   HOH HOH A . 
I 7 HOH 102 702  123 HOH HOH A . 
I 7 HOH 103 703  19  HOH HOH A . 
I 7 HOH 104 704  873 HOH HOH A . 
I 7 HOH 105 705  3   HOH HOH A . 
I 7 HOH 106 706  15  HOH HOH A . 
I 7 HOH 107 707  442 HOH HOH A . 
I 7 HOH 108 708  116 HOH HOH A . 
I 7 HOH 109 709  23  HOH HOH A . 
I 7 HOH 110 710  75  HOH HOH A . 
I 7 HOH 111 711  190 HOH HOH A . 
I 7 HOH 112 712  186 HOH HOH A . 
I 7 HOH 113 713  221 HOH HOH A . 
I 7 HOH 114 714  151 HOH HOH A . 
I 7 HOH 115 715  612 HOH HOH A . 
I 7 HOH 116 716  314 HOH HOH A . 
I 7 HOH 117 717  323 HOH HOH A . 
I 7 HOH 118 718  9   HOH HOH A . 
I 7 HOH 119 719  166 HOH HOH A . 
I 7 HOH 120 720  144 HOH HOH A . 
I 7 HOH 121 721  101 HOH HOH A . 
I 7 HOH 122 722  214 HOH HOH A . 
I 7 HOH 123 723  242 HOH HOH A . 
I 7 HOH 124 724  429 HOH HOH A . 
I 7 HOH 125 725  318 HOH HOH A . 
I 7 HOH 126 726  18  HOH HOH A . 
I 7 HOH 127 727  56  HOH HOH A . 
I 7 HOH 128 728  177 HOH HOH A . 
I 7 HOH 129 729  155 HOH HOH A . 
I 7 HOH 130 730  342 HOH HOH A . 
I 7 HOH 131 731  44  HOH HOH A . 
I 7 HOH 132 732  202 HOH HOH A . 
I 7 HOH 133 733  227 HOH HOH A . 
I 7 HOH 134 734  377 HOH HOH A . 
I 7 HOH 135 735  331 HOH HOH A . 
I 7 HOH 136 736  376 HOH HOH A . 
I 7 HOH 137 737  59  HOH HOH A . 
I 7 HOH 138 738  181 HOH HOH A . 
I 7 HOH 139 739  45  HOH HOH A . 
I 7 HOH 140 740  360 HOH HOH A . 
I 7 HOH 141 741  233 HOH HOH A . 
I 7 HOH 142 742  321 HOH HOH A . 
I 7 HOH 143 743  121 HOH HOH A . 
I 7 HOH 144 744  191 HOH HOH A . 
I 7 HOH 145 745  390 HOH HOH A . 
I 7 HOH 146 746  665 HOH HOH A . 
I 7 HOH 147 747  218 HOH HOH A . 
I 7 HOH 148 748  197 HOH HOH A . 
I 7 HOH 149 749  325 HOH HOH A . 
I 7 HOH 150 750  264 HOH HOH A . 
I 7 HOH 151 751  900 HOH HOH A . 
I 7 HOH 152 752  373 HOH HOH A . 
I 7 HOH 153 753  83  HOH HOH A . 
I 7 HOH 154 754  104 HOH HOH A . 
I 7 HOH 155 755  163 HOH HOH A . 
I 7 HOH 156 756  38  HOH HOH A . 
I 7 HOH 157 757  102 HOH HOH A . 
I 7 HOH 158 758  188 HOH HOH A . 
I 7 HOH 159 759  47  HOH HOH A . 
I 7 HOH 160 760  64  HOH HOH A . 
I 7 HOH 161 761  355 HOH HOH A . 
I 7 HOH 162 762  14  HOH HOH A . 
I 7 HOH 163 763  12  HOH HOH A . 
I 7 HOH 164 764  518 HOH HOH A . 
I 7 HOH 165 765  139 HOH HOH A . 
I 7 HOH 166 766  57  HOH HOH A . 
I 7 HOH 167 767  238 HOH HOH A . 
I 7 HOH 168 768  432 HOH HOH A . 
I 7 HOH 169 769  61  HOH HOH A . 
I 7 HOH 170 770  178 HOH HOH A . 
I 7 HOH 171 771  872 HOH HOH A . 
I 7 HOH 172 772  71  HOH HOH A . 
I 7 HOH 173 773  180 HOH HOH A . 
I 7 HOH 174 774  257 HOH HOH A . 
I 7 HOH 175 775  67  HOH HOH A . 
I 7 HOH 176 776  440 HOH HOH A . 
I 7 HOH 177 777  147 HOH HOH A . 
I 7 HOH 178 778  27  HOH HOH A . 
I 7 HOH 179 779  353 HOH HOH A . 
I 7 HOH 180 780  219 HOH HOH A . 
I 7 HOH 181 781  254 HOH HOH A . 
I 7 HOH 182 782  877 HOH HOH A . 
I 7 HOH 183 783  54  HOH HOH A . 
I 7 HOH 184 784  153 HOH HOH A . 
I 7 HOH 185 785  915 HOH HOH A . 
I 7 HOH 186 786  347 HOH HOH A . 
I 7 HOH 187 787  167 HOH HOH A . 
I 7 HOH 188 788  336 HOH HOH A . 
I 7 HOH 189 789  112 HOH HOH A . 
I 7 HOH 190 790  874 HOH HOH A . 
I 7 HOH 191 791  427 HOH HOH A . 
I 7 HOH 192 792  189 HOH HOH A . 
I 7 HOH 193 793  491 HOH HOH A . 
I 7 HOH 194 794  354 HOH HOH A . 
I 7 HOH 195 795  458 HOH HOH A . 
I 7 HOH 196 796  480 HOH HOH A . 
I 7 HOH 197 797  229 HOH HOH A . 
I 7 HOH 198 798  933 HOH HOH A . 
I 7 HOH 199 799  724 HOH HOH A . 
I 7 HOH 200 800  52  HOH HOH A . 
I 7 HOH 201 801  890 HOH HOH A . 
I 7 HOH 202 802  63  HOH HOH A . 
I 7 HOH 203 803  86  HOH HOH A . 
I 7 HOH 204 804  312 HOH HOH A . 
I 7 HOH 205 805  127 HOH HOH A . 
I 7 HOH 206 806  411 HOH HOH A . 
I 7 HOH 207 807  489 HOH HOH A . 
I 7 HOH 208 808  16  HOH HOH A . 
I 7 HOH 209 809  2   HOH HOH A . 
I 7 HOH 210 810  379 HOH HOH A . 
I 7 HOH 211 811  74  HOH HOH A . 
I 7 HOH 212 812  34  HOH HOH A . 
I 7 HOH 213 813  383 HOH HOH A . 
I 7 HOH 214 814  25  HOH HOH A . 
I 7 HOH 215 815  55  HOH HOH A . 
I 7 HOH 216 816  267 HOH HOH A . 
I 7 HOH 217 817  212 HOH HOH A . 
I 7 HOH 218 818  328 HOH HOH A . 
I 7 HOH 219 819  474 HOH HOH A . 
I 7 HOH 220 820  65  HOH HOH A . 
I 7 HOH 221 821  194 HOH HOH A . 
I 7 HOH 222 822  146 HOH HOH A . 
I 7 HOH 223 823  207 HOH HOH A . 
I 7 HOH 224 824  70  HOH HOH A . 
I 7 HOH 225 825  193 HOH HOH A . 
I 7 HOH 226 826  162 HOH HOH A . 
I 7 HOH 227 827  130 HOH HOH A . 
I 7 HOH 228 828  94  HOH HOH A . 
I 7 HOH 229 829  29  HOH HOH A . 
I 7 HOH 230 830  183 HOH HOH A . 
I 7 HOH 231 831  35  HOH HOH A . 
I 7 HOH 232 832  76  HOH HOH A . 
I 7 HOH 233 833  761 HOH HOH A . 
I 7 HOH 234 834  179 HOH HOH A . 
I 7 HOH 235 835  892 HOH HOH A . 
I 7 HOH 236 836  126 HOH HOH A . 
I 7 HOH 237 837  577 HOH HOH A . 
I 7 HOH 238 838  103 HOH HOH A . 
I 7 HOH 239 839  499 HOH HOH A . 
I 7 HOH 240 840  530 HOH HOH A . 
I 7 HOH 241 841  881 HOH HOH A . 
I 7 HOH 242 842  72  HOH HOH A . 
I 7 HOH 243 843  113 HOH HOH A . 
I 7 HOH 244 844  243 HOH HOH A . 
I 7 HOH 245 845  160 HOH HOH A . 
I 7 HOH 246 846  97  HOH HOH A . 
I 7 HOH 247 847  20  HOH HOH A . 
I 7 HOH 248 848  332 HOH HOH A . 
I 7 HOH 249 849  17  HOH HOH A . 
I 7 HOH 250 850  683 HOH HOH A . 
I 7 HOH 251 851  437 HOH HOH A . 
I 7 HOH 252 852  285 HOH HOH A . 
I 7 HOH 253 853  41  HOH HOH A . 
I 7 HOH 254 854  31  HOH HOH A . 
I 7 HOH 255 855  562 HOH HOH A . 
I 7 HOH 256 856  923 HOH HOH A . 
I 7 HOH 257 857  13  HOH HOH A . 
I 7 HOH 258 858  905 HOH HOH A . 
I 7 HOH 259 859  107 HOH HOH A . 
I 7 HOH 260 860  175 HOH HOH A . 
I 7 HOH 261 861  40  HOH HOH A . 
I 7 HOH 262 862  173 HOH HOH A . 
I 7 HOH 263 863  395 HOH HOH A . 
I 7 HOH 264 864  320 HOH HOH A . 
I 7 HOH 265 865  36  HOH HOH A . 
I 7 HOH 266 866  51  HOH HOH A . 
I 7 HOH 267 867  247 HOH HOH A . 
I 7 HOH 268 868  559 HOH HOH A . 
I 7 HOH 269 869  259 HOH HOH A . 
I 7 HOH 270 870  199 HOH HOH A . 
I 7 HOH 271 871  294 HOH HOH A . 
I 7 HOH 272 872  278 HOH HOH A . 
I 7 HOH 273 873  182 HOH HOH A . 
I 7 HOH 274 874  122 HOH HOH A . 
I 7 HOH 275 875  30  HOH HOH A . 
I 7 HOH 276 876  192 HOH HOH A . 
I 7 HOH 277 877  184 HOH HOH A . 
I 7 HOH 278 878  381 HOH HOH A . 
I 7 HOH 279 879  119 HOH HOH A . 
I 7 HOH 280 880  220 HOH HOH A . 
I 7 HOH 281 881  519 HOH HOH A . 
I 7 HOH 282 882  187 HOH HOH A . 
I 7 HOH 283 883  136 HOH HOH A . 
I 7 HOH 284 884  32  HOH HOH A . 
I 7 HOH 285 885  902 HOH HOH A . 
I 7 HOH 286 886  84  HOH HOH A . 
I 7 HOH 287 887  106 HOH HOH A . 
I 7 HOH 288 888  272 HOH HOH A . 
I 7 HOH 289 889  610 HOH HOH A . 
I 7 HOH 290 890  535 HOH HOH A . 
I 7 HOH 291 891  88  HOH HOH A . 
I 7 HOH 292 892  361 HOH HOH A . 
I 7 HOH 293 893  487 HOH HOH A . 
I 7 HOH 294 894  928 HOH HOH A . 
I 7 HOH 295 895  217 HOH HOH A . 
I 7 HOH 296 896  256 HOH HOH A . 
I 7 HOH 297 897  5   HOH HOH A . 
I 7 HOH 298 898  95  HOH HOH A . 
I 7 HOH 299 899  231 HOH HOH A . 
I 7 HOH 300 900  420 HOH HOH A . 
I 7 HOH 301 901  170 HOH HOH A . 
I 7 HOH 302 902  224 HOH HOH A . 
I 7 HOH 303 903  234 HOH HOH A . 
I 7 HOH 304 904  203 HOH HOH A . 
I 7 HOH 305 905  496 HOH HOH A . 
I 7 HOH 306 906  327 HOH HOH A . 
I 7 HOH 307 907  266 HOH HOH A . 
I 7 HOH 308 908  287 HOH HOH A . 
I 7 HOH 309 909  350 HOH HOH A . 
I 7 HOH 310 910  762 HOH HOH A . 
I 7 HOH 311 911  469 HOH HOH A . 
I 7 HOH 312 912  249 HOH HOH A . 
I 7 HOH 313 913  368 HOH HOH A . 
I 7 HOH 314 914  109 HOH HOH A . 
I 7 HOH 315 915  110 HOH HOH A . 
I 7 HOH 316 916  77  HOH HOH A . 
I 7 HOH 317 917  308 HOH HOH A . 
I 7 HOH 318 918  466 HOH HOH A . 
I 7 HOH 319 919  936 HOH HOH A . 
I 7 HOH 320 920  124 HOH HOH A . 
I 7 HOH 321 921  399 HOH HOH A . 
I 7 HOH 322 922  159 HOH HOH A . 
I 7 HOH 323 923  78  HOH HOH A . 
I 7 HOH 324 924  908 HOH HOH A . 
I 7 HOH 325 925  262 HOH HOH A . 
I 7 HOH 326 926  143 HOH HOH A . 
I 7 HOH 327 927  248 HOH HOH A . 
I 7 HOH 328 928  286 HOH HOH A . 
I 7 HOH 329 929  92  HOH HOH A . 
I 7 HOH 330 930  339 HOH HOH A . 
I 7 HOH 331 931  10  HOH HOH A . 
I 7 HOH 332 932  96  HOH HOH A . 
I 7 HOH 333 933  111 HOH HOH A . 
I 7 HOH 334 934  169 HOH HOH A . 
I 7 HOH 335 935  431 HOH HOH A . 
I 7 HOH 336 936  237 HOH HOH A . 
I 7 HOH 337 937  69  HOH HOH A . 
I 7 HOH 338 938  62  HOH HOH A . 
I 7 HOH 339 939  21  HOH HOH A . 
I 7 HOH 340 940  24  HOH HOH A . 
I 7 HOH 341 941  258 HOH HOH A . 
I 7 HOH 342 942  152 HOH HOH A . 
I 7 HOH 343 943  540 HOH HOH A . 
I 7 HOH 344 944  326 HOH HOH A . 
I 7 HOH 345 945  140 HOH HOH A . 
I 7 HOH 346 946  93  HOH HOH A . 
I 7 HOH 347 947  901 HOH HOH A . 
I 7 HOH 348 948  418 HOH HOH A . 
I 7 HOH 349 949  138 HOH HOH A . 
I 7 HOH 350 950  343 HOH HOH A . 
I 7 HOH 351 951  108 HOH HOH A . 
I 7 HOH 352 952  357 HOH HOH A . 
I 7 HOH 353 953  37  HOH HOH A . 
I 7 HOH 354 954  131 HOH HOH A . 
I 7 HOH 355 955  6   HOH HOH A . 
I 7 HOH 356 956  125 HOH HOH A . 
I 7 HOH 357 957  547 HOH HOH A . 
I 7 HOH 358 958  7   HOH HOH A . 
I 7 HOH 359 959  796 HOH HOH A . 
I 7 HOH 360 960  384 HOH HOH A . 
I 7 HOH 361 961  161 HOH HOH A . 
I 7 HOH 362 962  66  HOH HOH A . 
I 7 HOH 363 963  117 HOH HOH A . 
I 7 HOH 364 964  58  HOH HOH A . 
I 7 HOH 365 965  931 HOH HOH A . 
I 7 HOH 366 966  359 HOH HOH A . 
I 7 HOH 367 967  910 HOH HOH A . 
I 7 HOH 368 968  550 HOH HOH A . 
I 7 HOH 369 969  11  HOH HOH A . 
I 7 HOH 370 970  68  HOH HOH A . 
I 7 HOH 371 971  277 HOH HOH A . 
I 7 HOH 372 972  105 HOH HOH A . 
I 7 HOH 373 973  171 HOH HOH A . 
I 7 HOH 374 974  228 HOH HOH A . 
I 7 HOH 375 975  311 HOH HOH A . 
I 7 HOH 376 976  758 HOH HOH A . 
I 7 HOH 377 977  43  HOH HOH A . 
I 7 HOH 378 978  501 HOH HOH A . 
I 7 HOH 379 979  895 HOH HOH A . 
I 7 HOH 380 980  584 HOH HOH A . 
I 7 HOH 381 981  389 HOH HOH A . 
I 7 HOH 382 982  904 HOH HOH A . 
I 7 HOH 383 983  335 HOH HOH A . 
I 7 HOH 384 984  141 HOH HOH A . 
I 7 HOH 385 985  914 HOH HOH A . 
I 7 HOH 386 986  891 HOH HOH A . 
I 7 HOH 387 987  790 HOH HOH A . 
I 7 HOH 388 988  502 HOH HOH A . 
I 7 HOH 389 989  164 HOH HOH A . 
I 7 HOH 390 990  260 HOH HOH A . 
I 7 HOH 391 991  783 HOH HOH A . 
I 7 HOH 392 992  53  HOH HOH A . 
I 7 HOH 393 993  299 HOH HOH A . 
I 7 HOH 394 994  364 HOH HOH A . 
I 7 HOH 395 995  906 HOH HOH A . 
I 7 HOH 396 996  98  HOH HOH A . 
I 7 HOH 397 997  261 HOH HOH A . 
I 7 HOH 398 998  832 HOH HOH A . 
I 7 HOH 399 999  85  HOH HOH A . 
I 7 HOH 400 1000 875 HOH HOH A . 
I 7 HOH 401 1001 28  HOH HOH A . 
I 7 HOH 402 1002 913 HOH HOH A . 
I 7 HOH 403 1003 781 HOH HOH A . 
I 7 HOH 404 1004 33  HOH HOH A . 
I 7 HOH 405 1005 426 HOH HOH A . 
I 7 HOH 406 1006 618 HOH HOH A . 
I 7 HOH 407 1007 899 HOH HOH A . 
I 7 HOH 408 1008 841 HOH HOH A . 
I 7 HOH 409 1009 129 HOH HOH A . 
I 7 HOH 410 1010 504 HOH HOH A . 
I 7 HOH 411 1011 281 HOH HOH A . 
I 7 HOH 412 1012 90  HOH HOH A . 
I 7 HOH 413 1013 451 HOH HOH A . 
I 7 HOH 414 1014 636 HOH HOH A . 
I 7 HOH 415 1015 527 HOH HOH A . 
I 7 HOH 416 1016 158 HOH HOH A . 
I 7 HOH 417 1017 337 HOH HOH A . 
I 7 HOH 418 1018 771 HOH HOH A . 
I 7 HOH 419 1019 409 HOH HOH A . 
I 7 HOH 420 1020 240 HOH HOH A . 
I 7 HOH 421 1021 333 HOH HOH A . 
I 7 HOH 422 1022 929 HOH HOH A . 
I 7 HOH 423 1023 275 HOH HOH A . 
I 7 HOH 424 1024 301 HOH HOH A . 
I 7 HOH 425 1025 857 HOH HOH A . 
I 7 HOH 426 1026 898 HOH HOH A . 
I 7 HOH 427 1027 424 HOH HOH A . 
I 7 HOH 428 1028 794 HOH HOH A . 
I 7 HOH 429 1029 751 HOH HOH A . 
I 7 HOH 430 1030 356 HOH HOH A . 
I 7 HOH 431 1031 302 HOH HOH A . 
I 7 HOH 432 1032 633 HOH HOH A . 
I 7 HOH 433 1033 270 HOH HOH A . 
I 7 HOH 434 1034 886 HOH HOH A . 
I 7 HOH 435 1035 903 HOH HOH A . 
I 7 HOH 436 1036 283 HOH HOH A . 
I 7 HOH 437 1037 196 HOH HOH A . 
I 7 HOH 438 1038 505 HOH HOH A . 
I 7 HOH 439 1039 290 HOH HOH A . 
I 7 HOH 440 1040 894 HOH HOH A . 
I 7 HOH 441 1041 769 HOH HOH A . 
I 7 HOH 442 1042 590 HOH HOH A . 
I 7 HOH 443 1043 406 HOH HOH A . 
I 7 HOH 444 1044 269 HOH HOH A . 
I 7 HOH 445 1045 289 HOH HOH A . 
I 7 HOH 446 1046 763 HOH HOH A . 
I 7 HOH 447 1047 222 HOH HOH A . 
I 7 HOH 448 1048 396 HOH HOH A . 
I 7 HOH 449 1049 422 HOH HOH A . 
I 7 HOH 450 1050 401 HOH HOH A . 
I 7 HOH 451 1051 784 HOH HOH A . 
I 7 HOH 452 1052 132 HOH HOH A . 
I 7 HOH 453 1053 438 HOH HOH A . 
I 7 HOH 454 1054 410 HOH HOH A . 
I 7 HOH 455 1055 271 HOH HOH A . 
I 7 HOH 456 1056 578 HOH HOH A . 
I 7 HOH 457 1057 490 HOH HOH A . 
I 7 HOH 458 1058 861 HOH HOH A . 
I 7 HOH 459 1059 921 HOH HOH A . 
I 7 HOH 460 1060 748 HOH HOH A . 
I 7 HOH 461 1061 777 HOH HOH A . 
I 7 HOH 462 1062 822 HOH HOH A . 
I 7 HOH 463 1063 919 HOH HOH A . 
I 7 HOH 464 1064 800 HOH HOH A . 
I 7 HOH 465 1065 87  HOH HOH A . 
I 7 HOH 466 1066 479 HOH HOH A . 
I 7 HOH 467 1067 917 HOH HOH A . 
I 7 HOH 468 1068 135 HOH HOH A . 
I 7 HOH 469 1069 165 HOH HOH A . 
I 7 HOH 470 1070 926 HOH HOH A . 
I 7 HOH 471 1071 239 HOH HOH A . 
I 7 HOH 472 1072 241 HOH HOH A . 
I 7 HOH 473 1073 473 HOH HOH A . 
I 7 HOH 474 1074 415 HOH HOH A . 
I 7 HOH 475 1075 774 HOH HOH A . 
I 7 HOH 476 1076 149 HOH HOH A . 
I 7 HOH 477 1077 767 HOH HOH A . 
I 7 HOH 478 1078 741 HOH HOH A . 
I 7 HOH 479 1079 273 HOH HOH A . 
I 7 HOH 480 1080 100 HOH HOH A . 
I 7 HOH 481 1081 907 HOH HOH A . 
I 7 HOH 482 1082 465 HOH HOH A . 
I 7 HOH 483 1083 298 HOH HOH A . 
I 7 HOH 484 1084 322 HOH HOH A . 
I 7 HOH 485 1085 91  HOH HOH A . 
I 7 HOH 486 1086 893 HOH HOH A . 
I 7 HOH 487 1087 475 HOH HOH A . 
I 7 HOH 488 1088 816 HOH HOH A . 
I 7 HOH 489 1089 211 HOH HOH A . 
I 7 HOH 490 1090 768 HOH HOH A . 
I 7 HOH 491 1091 742 HOH HOH A . 
I 7 HOH 492 1092 503 HOH HOH A . 
I 7 HOH 493 1093 22  HOH HOH A . 
I 7 HOH 494 1094 765 HOH HOH A . 
I 7 HOH 495 1095 927 HOH HOH A . 
I 7 HOH 496 1096 225 HOH HOH A . 
I 7 HOH 497 1097 439 HOH HOH A . 
I 7 HOH 498 1098 380 HOH HOH A . 
I 7 HOH 499 1099 660 HOH HOH A . 
I 7 HOH 500 1100 134 HOH HOH A . 
I 7 HOH 501 1101 394 HOH HOH A . 
I 7 HOH 502 1102 852 HOH HOH A . 
I 7 HOH 503 1103 366 HOH HOH A . 
I 7 HOH 504 1104 776 HOH HOH A . 
I 7 HOH 505 1105 772 HOH HOH A . 
I 7 HOH 506 1106 306 HOH HOH A . 
I 7 HOH 507 1107 909 HOH HOH A . 
I 7 HOH 508 1108 244 HOH HOH A . 
I 7 HOH 509 1109 863 HOH HOH A . 
I 7 HOH 510 1110 282 HOH HOH A . 
I 7 HOH 511 1111 925 HOH HOH A . 
I 7 HOH 512 1112 766 HOH HOH A . 
I 7 HOH 513 1113 775 HOH HOH A . 
I 7 HOH 514 1114 348 HOH HOH A . 
I 7 HOH 515 1115 740 HOH HOH A . 
I 7 HOH 516 1116 754 HOH HOH A . 
I 7 HOH 517 1117 789 HOH HOH A . 
I 7 HOH 518 1118 880 HOH HOH A . 
I 7 HOH 519 1119 421 HOH HOH A . 
I 7 HOH 520 1120 524 HOH HOH A . 
I 7 HOH 521 1121 744 HOH HOH A . 
I 7 HOH 522 1122 447 HOH HOH A . 
I 7 HOH 523 1123 514 HOH HOH A . 
I 7 HOH 524 1124 642 HOH HOH A . 
I 7 HOH 525 1125 145 HOH HOH A . 
I 7 HOH 526 1126 367 HOH HOH A . 
I 7 HOH 527 1127 788 HOH HOH A . 
I 7 HOH 528 1128 482 HOH HOH A . 
I 7 HOH 529 1129 156 HOH HOH A . 
I 7 HOH 530 1130 537 HOH HOH A . 
I 7 HOH 531 1131 752 HOH HOH A . 
I 7 HOH 532 1132 757 HOH HOH A . 
I 7 HOH 533 1133 528 HOH HOH A . 
I 7 HOH 534 1134 400 HOH HOH A . 
I 7 HOH 535 1135 316 HOH HOH A . 
I 7 HOH 536 1136 609 HOH HOH A . 
I 7 HOH 537 1137 81  HOH HOH A . 
I 7 HOH 538 1138 288 HOH HOH A . 
I 7 HOH 539 1139 869 HOH HOH A . 
I 7 HOH 540 1140 276 HOH HOH A . 
I 7 HOH 541 1141 291 HOH HOH A . 
I 7 HOH 542 1142 747 HOH HOH A . 
I 7 HOH 543 1143 779 HOH HOH A . 
I 7 HOH 544 1144 407 HOH HOH A . 
I 7 HOH 545 1145 386 HOH HOH A . 
I 7 HOH 546 1146 760 HOH HOH A . 
I 7 HOH 547 1147 393 HOH HOH A . 
I 7 HOH 548 1148 745 HOH HOH A . 
I 7 HOH 549 1149 876 HOH HOH A . 
I 7 HOH 550 1150 587 HOH HOH A . 
I 7 HOH 551 1151 787 HOH HOH A . 
I 7 HOH 552 1152 226 HOH HOH A . 
I 7 HOH 553 1153 739 HOH HOH A . 
I 7 HOH 554 1154 375 HOH HOH A . 
I 7 HOH 555 1155 456 HOH HOH A . 
I 7 HOH 556 1156 648 HOH HOH A . 
I 7 HOH 557 1157 459 HOH HOH A . 
I 7 HOH 558 1158 815 HOH HOH A . 
I 7 HOH 559 1159 579 HOH HOH A . 
I 7 HOH 560 1160 497 HOH HOH A . 
I 7 HOH 561 1161 780 HOH HOH A . 
I 7 HOH 562 1162 344 HOH HOH A . 
I 7 HOH 563 1163 865 HOH HOH A . 
I 7 HOH 564 1164 619 HOH HOH A . 
I 7 HOH 565 1165 293 HOH HOH A . 
I 7 HOH 566 1166 884 HOH HOH A . 
I 7 HOH 567 1167 358 HOH HOH A . 
I 7 HOH 568 1168 268 HOH HOH A . 
I 7 HOH 569 1169 372 HOH HOH A . 
I 7 HOH 570 1170 404 HOH HOH A . 
I 7 HOH 571 1171 313 HOH HOH A . 
I 7 HOH 572 1172 834 HOH HOH A . 
I 7 HOH 573 1173 749 HOH HOH A . 
I 7 HOH 574 1174 911 HOH HOH A . 
I 7 HOH 575 1175 517 HOH HOH A . 
I 7 HOH 576 1176 746 HOH HOH A . 
I 7 HOH 577 1177 888 HOH HOH A . 
I 7 HOH 578 1178 309 HOH HOH A . 
I 7 HOH 579 1179 246 HOH HOH A . 
I 7 HOH 580 1180 507 HOH HOH A . 
I 7 HOH 581 1181 120 HOH HOH A . 
I 7 HOH 582 1182 932 HOH HOH A . 
I 7 HOH 583 1183 793 HOH HOH A . 
I 7 HOH 584 1184 296 HOH HOH A . 
I 7 HOH 585 1185 791 HOH HOH A . 
I 7 HOH 586 1186 462 HOH HOH A . 
I 7 HOH 587 1187 738 HOH HOH A . 
I 7 HOH 588 1188 606 HOH HOH A . 
I 7 HOH 589 1189 274 HOH HOH A . 
I 7 HOH 590 1190 8   HOH HOH A . 
I 7 HOH 591 1191 922 HOH HOH A . 
I 7 HOH 592 1192 346 HOH HOH A . 
I 7 HOH 593 1193 245 HOH HOH A . 
I 7 HOH 594 1194 795 HOH HOH A . 
I 7 HOH 595 1195 797 HOH HOH A . 
I 7 HOH 596 1196 867 HOH HOH A . 
I 7 HOH 597 1197 634 HOH HOH A . 
I 7 HOH 598 1198 251 HOH HOH A . 
I 7 HOH 599 1199 828 HOH HOH A . 
I 7 HOH 600 1200 782 HOH HOH A . 
I 7 HOH 601 1202 690 HOH HOH A . 
I 7 HOH 602 1204 854 HOH HOH A . 
I 7 HOH 603 1205 750 HOH HOH A . 
I 7 HOH 604 1206 778 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A THR 291 ? OG1 ? A THR 291 OG1 
2 1 Y 1 A THR 291 ? CG2 ? A THR 291 CG2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H92 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     65.115 
_cell.length_a_esd                 ? 
_cell.length_b                     115.720 
_cell.length_b_esd                 ? 
_cell.length_c                     137.426 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9H92 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9H92 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.57 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.07 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M K thiocyanate, 20 % PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.96546 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.96546 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H92 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.55 
_reflns.d_resolution_low                               137.43 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     75455 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.01 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.186 
_reflns.pdbx_Rpim_I_all                                0.072 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       494466 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.171 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.55 
_reflns_shell.d_res_low                                     1.58 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           21068 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3698 
_reflns_shell.percent_possible_obs                          100.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               5.7 
_reflns_shell.pdbx_chi_squared                              1.01 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.0 
_reflns_shell.pdbx_Rrim_I_all                               1.747 
_reflns_shell.pdbx_Rpim_I_all                               0.726 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.578 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.586 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.13 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            1.69 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.56 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               16.007 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.956 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9H92 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.55 
_refine.ls_d_res_low                             68.71 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     71628 
_refine.ls_number_reflns_R_free                  3781 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.98 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17040 
_refine.ls_R_factor_R_free                       0.20161 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16880 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.075 
_refine.pdbx_overall_ESU_R_Free                  0.078 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.011 
_refine.overall_SU_ML                            0.066 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        68.71 
_refine_hist.number_atoms_solvent             607 
_refine_hist.number_atoms_total               4323 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3526 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         190 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  0.012  3821 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3376 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.750  1.800  5233 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.917  1.720  7786 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.455  5.000  467  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 4.935  5.000  14   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.226 10.000 518  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.159  0.200  608  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  4495 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  890  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.299  1.550  1867 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.298  1.548  1865 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.763  2.778  2330 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.763  2.779  2331 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.816  1.948  1954 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.791  1.948  1953 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.231  3.439  2901 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.656  19.64  4610 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.328  17.19  4411 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.550 
_refine_ls_shell.d_res_low                        1.590 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             284 
_refine_ls_shell.number_reflns_R_work             5241 
_refine_ls_shell.percent_reflns_obs               99.98 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.310 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.334 
# 
_struct.entry_id                     9H92 
_struct.title                        'FAD-dependent oxidase sorD' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9H92 
_struct_keywords.text            'Flavin, FAD, natural product, oxidase, sorbicillinoids, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 6 ? 
I N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SORD_PENRW 
_struct_ref.pdbx_db_accession          B6HNK6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MQAASAFATCLLASVGGNSSAVAFPNQANYSTLVAPYNFDLLTTPSAIVWPQDTQQVAAAVKCAVDSDIKVQPKSGGHNY
GNYGSTTGELSVNLDNLQHFSMDETSWTARLGPGNRLGRVTELMYNNGGRHVPHGTTFTVGLGGHATVGGAGAASRMHGL
LLDYVEEVEVVLANSSIVRASKSHNEDLFFAVRGAASSVGIVTDFSIRTEPVPVSSVTYSYIWEGTDPAARAEVFLTWQS
LLAGGSLPQHMAYDLVATANSMILGGAYFGSQEDFEAFNLSSHFKVAPDVAHIKTYTNFFDFSAAASAQTKAAGIASPSH
FYAKSLVFNQQTLIPDDAAEEVFKYLATTKNGTDLYAVTFAALGGAVRDVSASETAFYHRDASYFMFSFGRTSGDLTDTT
VQFLDGLSEVLTSGQPDAYYGQYVGNVDPRQSTDKALTGYYGKNLHRLQQIKSAVDPNDVFHNQQSIPPLS
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9H92 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 471 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             B6HNK6 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  471 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       471 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9H92 ASN A 103 ? UNP B6HNK6 ASP 103 conflict 103 1 
1 9H92 THR A 291 ? UNP B6HNK6 ALA 291 conflict 291 2 
1 9H92 PRO A 432 ? UNP B6HNK6 SER 432 conflict 432 3 
1 9H92 GLU A 435 ? UNP B6HNK6 LYS 435 conflict 435 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4200  ? 
1 MORE         23    ? 
1 'SSA (A^2)'  18330 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 5   ? VAL A 15  ? SER A 5   VAL A 15  1 ? 11 
HELX_P HELX_P2  AA2 ASN A 18  ? SER A 20  ? ASN A 18  SER A 20  5 ? 3  
HELX_P HELX_P3  AA3 ASN A 29  ? ALA A 35  ? ASN A 29  ALA A 35  1 ? 7  
HELX_P HELX_P4  AA4 ASP A 53  ? SER A 67  ? ASP A 53  SER A 67  1 ? 15 
HELX_P HELX_P5  AA5 ASN A 82  ? THR A 86  ? ASN A 82  THR A 86  5 ? 5  
HELX_P HELX_P6  AA6 ARG A 116 ? ASN A 127 ? ARG A 116 ASN A 127 1 ? 12 
HELX_P HELX_P7  AA7 GLY A 141 ? ALA A 146 ? GLY A 141 ALA A 146 1 ? 6  
HELX_P HELX_P8  AA8 ALA A 154 ? GLY A 159 ? ALA A 154 GLY A 159 1 ? 6  
HELX_P HELX_P9  AA9 LEU A 160 ? ASP A 163 ? LEU A 160 ASP A 163 5 ? 4  
HELX_P HELX_P10 AB1 ASN A 185 ? ALA A 196 ? ASN A 185 ALA A 196 1 ? 12 
HELX_P HELX_P11 AB2 SER A 197 ? VAL A 199 ? SER A 197 VAL A 199 5 ? 3  
HELX_P HELX_P12 AB3 ASP A 227 ? GLY A 244 ? ASP A 227 GLY A 244 1 ? 18 
HELX_P HELX_P13 AB4 SER A 271 ? ASN A 279 ? SER A 271 ASN A 279 1 ? 9  
HELX_P HELX_P14 AB5 LEU A 280 ? PHE A 284 ? LEU A 280 PHE A 284 5 ? 5  
HELX_P HELX_P15 AB6 ASN A 298 ? ALA A 313 ? ASN A 298 ALA A 313 1 ? 16 
HELX_P HELX_P16 AB7 PRO A 335 ? THR A 349 ? PRO A 335 THR A 349 1 ? 15 
HELX_P HELX_P17 AB8 GLY A 364 ? VAL A 370 ? GLY A 364 VAL A 370 5 ? 7  
HELX_P HELX_P18 AB9 THR A 397 ? THR A 412 ? THR A 397 THR A 412 1 ? 16 
HELX_P HELX_P19 AC1 PRO A 432 ? GLY A 442 ? PRO A 432 GLY A 442 1 ? 11 
HELX_P HELX_P20 AC2 ASN A 444 ? ASP A 456 ? ASN A 444 ASP A 456 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 10  SG  ? ? ? 1_555 A CYS 63 SG  ? ? A CYS 10  A CYS 63  1_555 ? ? ? ? ? ? ? 2.374 ? ?               
covale1  covale one  ? A ASN 18  ND2 ? ? ? 1_555 D NAG .  C1  ? ? A ASN 18  D NAG 1   1_555 ? ? ? ? ? ? ? 1.438 ? N-Glycosylation 
covale2  covale one  ? A ASN 29  ND2 ? ? ? 1_555 F NAG .  C1  ? ? A ASN 29  A NAG 502 1_555 ? ? ? ? ? ? ? 1.450 ? N-Glycosylation 
covale3  covale none ? A HIS 78  ND1 ? ? ? 1_555 E FAD .  C8M ? ? A HIS 78  A FAD 501 1_555 ? ? ? ? ? ? ? 1.519 ? ?               
covale4  covale one  ? A ASN 174 ND2 ? ? ? 1_555 C NAG .  C1  ? ? A ASN 174 C NAG 1   1_555 ? ? ? ? ? ? ? 1.449 ? N-Glycosylation 
covale5  covale one  ? A ASN 279 ND2 ? ? ? 1_555 G NAG .  C1  ? ? A ASN 279 A NAG 503 1_555 ? ? ? ? ? ? ? 1.457 ? N-Glycosylation 
covale6  covale one  ? A ASN 351 ND2 ? ? ? 1_555 B NAG .  C1  ? ? A ASN 351 B NAG 1   1_555 ? ? ? ? ? ? ? 1.471 ? N-Glycosylation 
covale7  covale both ? B NAG .   O4  ? ? ? 1_555 B NAG .  C1  ? ? B NAG 1   B NAG 2   1_555 ? ? ? ? ? ? ? 1.392 ? ?               
covale8  covale both ? B NAG .   O4  ? ? ? 1_555 B MAN .  C1  ? ? B NAG 2   B MAN 3   1_555 ? ? ? ? ? ? ? 1.392 ? ?               
covale9  covale both ? B MAN .   O6  ? ? ? 1_555 B MAN .  C1  ? ? B MAN 3   B MAN 4   1_555 ? ? ? ? ? ? ? 1.408 ? ?               
covale10 covale both ? C NAG .   O4  ? ? ? 1_555 C NAG .  C1  ? ? C NAG 1   C NAG 2   1_555 ? ? ? ? ? ? ? 1.392 ? ?               
covale11 covale both ? D NAG .   O4  ? ? ? 1_555 D NAG .  C1  ? ? D NAG 1   D NAG 2   1_555 ? ? ? ? ? ? ? 1.392 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG B .  ? ASN A 351 ? NAG B 1   ? 1_555 ASN A 351 ? 1_555 C1  ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG C .  ? ASN A 174 ? NAG C 1   ? 1_555 ASN A 174 ? 1_555 C1  ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 NAG D .  ? ASN A 18  ? NAG D 1   ? 1_555 ASN A 18  ? 1_555 C1  ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4 NAG F .  ? ASN A 29  ? NAG A 502 ? 1_555 ASN A 29  ? 1_555 C1  ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5 NAG G .  ? ASN A 279 ? NAG A 503 ? 1_555 ASN A 279 ? 1_555 C1  ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6 FAD E .  ? HIS A 78  ? FAD A 501 ? 1_555 HIS A 78  ? 1_555 C8M ND1 HIS 2 FAD None            Flavin             
7 CYS A 10 ? CYS A 63  ? CYS A 10  ? 1_555 CYS A 63  ? 1_555 SG  SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 22  ? ALA A 23  ? VAL A 22  ALA A 23  
AA1 2 ALA A 47  ? VAL A 49  ? ALA A 47  VAL A 49  
AA1 3 LEU A 90  ? ASN A 93  ? LEU A 90  ASN A 93  
AA1 4 VAL A 71  ? LYS A 74  ? VAL A 71  LYS A 74  
AA2 1 PHE A 100 ? ASN A 103 ? PHE A 100 ASN A 103 
AA2 2 THR A 108 ? LEU A 111 ? THR A 108 LEU A 111 
AA2 3 ILE A 201 ? ARG A 208 ? ILE A 201 ARG A 208 
AA2 4 VAL A 165 ? VAL A 171 ? VAL A 165 VAL A 171 
AA2 5 ILE A 177 ? ALA A 180 ? ILE A 177 ALA A 180 
AA3 1 ARG A 130 ? HIS A 131 ? ARG A 130 HIS A 131 
AA3 2 GLU A 210 ? PRO A 211 ? GLU A 210 PRO A 211 
AA4 1 VAL A 290 ? TYR A 296 ? VAL A 290 TYR A 296 
AA4 2 SER A 216 ? GLU A 224 ? SER A 216 GLU A 224 
AA4 3 SER A 261 ? TYR A 268 ? SER A 261 TYR A 268 
AA4 4 ALA A 252 ? ALA A 257 ? ALA A 252 ALA A 257 
AA4 5 LEU A 355 ? ALA A 362 ? LEU A 355 ALA A 362 
AA4 6 TYR A 384 ? THR A 392 ? TYR A 384 THR A 392 
AA4 7 HIS A 320 ? PHE A 328 ? HIS A 320 PHE A 328 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ALA A 23  ? N ALA A 23  O ILE A 48  ? O ILE A 48  
AA1 2 3 N ALA A 47  ? N ALA A 47  O SER A 91  ? O SER A 91  
AA1 3 4 O VAL A 92  ? O VAL A 92  N LYS A 74  ? N LYS A 74  
AA2 1 2 N SER A 101 ? N SER A 101 O ARG A 110 ? O ARG A 110 
AA2 2 3 N ALA A 109 ? N ALA A 109 O ILE A 207 ? O ILE A 207 
AA2 3 4 O SER A 206 ? O SER A 206 N GLU A 166 ? N GLU A 166 
AA2 4 5 N VAL A 170 ? N VAL A 170 O VAL A 178 ? O VAL A 178 
AA3 1 2 N HIS A 131 ? N HIS A 131 O GLU A 210 ? O GLU A 210 
AA4 1 2 O VAL A 290 ? O VAL A 290 N ILE A 222 ? N ILE A 222 
AA4 2 3 N VAL A 217 ? N VAL A 217 O TYR A 268 ? O TYR A 268 
AA4 3 4 O GLY A 265 ? O GLY A 265 N ASP A 254 ? N ASP A 254 
AA4 4 5 N LEU A 255 ? N LEU A 255 O PHE A 360 ? O PHE A 360 
AA4 5 6 N THR A 359 ? N THR A 359 O PHE A 387 ? O PHE A 387 
AA4 6 7 O GLY A 390 ? O GLY A 390 N TYR A 322 ? N TYR A 322 
# 
_pdbx_entry_details.entry_id                   9H92 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 26  ? ? 84.50   -0.04   
2 1 ALA A 35  ? ? 60.40   63.51   
3 1 TRP A 50  ? ? -117.44 78.06   
4 1 SER A 75  ? ? -106.55 -77.05  
5 1 ALA A 195 ? ? -144.84 29.34   
6 1 LEU A 363 ? ? -115.21 -152.32 
7 1 HIS A 379 ? ? -86.69  42.38   
8 1 GLN A 415 ? ? -153.25 73.23   
9 1 ARG A 430 ? ? -99.88  55.40   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 656  ? I HOH . 
2 1 A HOH 790  ? I HOH . 
3 1 A HOH 830  ? I HOH . 
4 1 A HOH 1013 ? I HOH . 
5 1 A HOH 1042 ? I HOH . 
6 1 A HOH 1140 ? I HOH . 
7 1 A HOH 1161 ? I HOH . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1200 ? 6.44 . 
2 1 O ? A HOH 1204 ? 7.28 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1   ? A MET 1   
2 1 Y 1 A GLN 2   ? A GLN 2   
3 1 Y 1 A ALA 3   ? A ALA 3   
4 1 Y 1 A ALA 4   ? A ALA 4   
5 1 Y 1 A SER 471 ? A SER 471 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FAD PA     P N R 88  
FAD O1A    O N N 89  
FAD O2A    O N N 90  
FAD O5B    O N N 91  
FAD C5B    C N N 92  
FAD C4B    C N R 93  
FAD O4B    O N N 94  
FAD C3B    C N S 95  
FAD O3B    O N N 96  
FAD C2B    C N R 97  
FAD O2B    O N N 98  
FAD C1B    C N R 99  
FAD N9A    N Y N 100 
FAD C8A    C Y N 101 
FAD N7A    N Y N 102 
FAD C5A    C Y N 103 
FAD C6A    C Y N 104 
FAD N6A    N N N 105 
FAD N1A    N Y N 106 
FAD C2A    C Y N 107 
FAD N3A    N Y N 108 
FAD C4A    C Y N 109 
FAD N1     N N N 110 
FAD C2     C N N 111 
FAD O2     O N N 112 
FAD N3     N N N 113 
FAD C4     C N N 114 
FAD O4     O N N 115 
FAD C4X    C N N 116 
FAD N5     N N N 117 
FAD C5X    C Y N 118 
FAD C6     C Y N 119 
FAD C7     C Y N 120 
FAD C7M    C N N 121 
FAD C8     C Y N 122 
FAD C8M    C N N 123 
FAD C9     C Y N 124 
FAD C9A    C Y N 125 
FAD N10    N N N 126 
FAD C10    C N N 127 
FAD "C1'"  C N N 128 
FAD "C2'"  C N S 129 
FAD "O2'"  O N N 130 
FAD "C3'"  C N S 131 
FAD "O3'"  O N N 132 
FAD "C4'"  C N R 133 
FAD "O4'"  O N N 134 
FAD "C5'"  C N N 135 
FAD "O5'"  O N N 136 
FAD P      P N R 137 
FAD O1P    O N N 138 
FAD O2P    O N N 139 
FAD O3P    O N N 140 
FAD HOA2   H N N 141 
FAD H51A   H N N 142 
FAD H52A   H N N 143 
FAD H4B    H N N 144 
FAD H3B    H N N 145 
FAD HO3A   H N N 146 
FAD H2B    H N N 147 
FAD HO2A   H N N 148 
FAD H1B    H N N 149 
FAD H8A    H N N 150 
FAD H61A   H N N 151 
FAD H62A   H N N 152 
FAD H2A    H N N 153 
FAD HN3    H N N 154 
FAD H6     H N N 155 
FAD HM71   H N N 156 
FAD HM72   H N N 157 
FAD HM73   H N N 158 
FAD HM81   H N N 159 
FAD HM82   H N N 160 
FAD HM83   H N N 161 
FAD H9     H N N 162 
FAD "H1'1" H N N 163 
FAD "H1'2" H N N 164 
FAD "H2'"  H N N 165 
FAD "HO2'" H N N 166 
FAD "H3'"  H N N 167 
FAD "HO3'" H N N 168 
FAD "H4'"  H N N 169 
FAD "HO4'" H N N 170 
FAD "H5'1" H N N 171 
FAD "H5'2" H N N 172 
FAD HOP2   H N N 173 
GLN N      N N N 174 
GLN CA     C N S 175 
GLN C      C N N 176 
GLN O      O N N 177 
GLN CB     C N N 178 
GLN CG     C N N 179 
GLN CD     C N N 180 
GLN OE1    O N N 181 
GLN NE2    N N N 182 
GLN OXT    O N N 183 
GLN H      H N N 184 
GLN H2     H N N 185 
GLN HA     H N N 186 
GLN HB2    H N N 187 
GLN HB3    H N N 188 
GLN HG2    H N N 189 
GLN HG3    H N N 190 
GLN HE21   H N N 191 
GLN HE22   H N N 192 
GLN HXT    H N N 193 
GLU N      N N N 194 
GLU CA     C N S 195 
GLU C      C N N 196 
GLU O      O N N 197 
GLU CB     C N N 198 
GLU CG     C N N 199 
GLU CD     C N N 200 
GLU OE1    O N N 201 
GLU OE2    O N N 202 
GLU OXT    O N N 203 
GLU H      H N N 204 
GLU H2     H N N 205 
GLU HA     H N N 206 
GLU HB2    H N N 207 
GLU HB3    H N N 208 
GLU HG2    H N N 209 
GLU HG3    H N N 210 
GLU HE2    H N N 211 
GLU HXT    H N N 212 
GLY N      N N N 213 
GLY CA     C N N 214 
GLY C      C N N 215 
GLY O      O N N 216 
GLY OXT    O N N 217 
GLY H      H N N 218 
GLY H2     H N N 219 
GLY HA2    H N N 220 
GLY HA3    H N N 221 
GLY HXT    H N N 222 
HIS N      N N N 223 
HIS CA     C N S 224 
HIS C      C N N 225 
HIS O      O N N 226 
HIS CB     C N N 227 
HIS CG     C Y N 228 
HIS ND1    N Y N 229 
HIS CD2    C Y N 230 
HIS CE1    C Y N 231 
HIS NE2    N Y N 232 
HIS OXT    O N N 233 
HIS H      H N N 234 
HIS H2     H N N 235 
HIS HA     H N N 236 
HIS HB2    H N N 237 
HIS HB3    H N N 238 
HIS HD1    H N N 239 
HIS HD2    H N N 240 
HIS HE1    H N N 241 
HIS HE2    H N N 242 
HIS HXT    H N N 243 
HOH O      O N N 244 
HOH H1     H N N 245 
HOH H2     H N N 246 
ILE N      N N N 247 
ILE CA     C N S 248 
ILE C      C N N 249 
ILE O      O N N 250 
ILE CB     C N S 251 
ILE CG1    C N N 252 
ILE CG2    C N N 253 
ILE CD1    C N N 254 
ILE OXT    O N N 255 
ILE H      H N N 256 
ILE H2     H N N 257 
ILE HA     H N N 258 
ILE HB     H N N 259 
ILE HG12   H N N 260 
ILE HG13   H N N 261 
ILE HG21   H N N 262 
ILE HG22   H N N 263 
ILE HG23   H N N 264 
ILE HD11   H N N 265 
ILE HD12   H N N 266 
ILE HD13   H N N 267 
ILE HXT    H N N 268 
LEU N      N N N 269 
LEU CA     C N S 270 
LEU C      C N N 271 
LEU O      O N N 272 
LEU CB     C N N 273 
LEU CG     C N N 274 
LEU CD1    C N N 275 
LEU CD2    C N N 276 
LEU OXT    O N N 277 
LEU H      H N N 278 
LEU H2     H N N 279 
LEU HA     H N N 280 
LEU HB2    H N N 281 
LEU HB3    H N N 282 
LEU HG     H N N 283 
LEU HD11   H N N 284 
LEU HD12   H N N 285 
LEU HD13   H N N 286 
LEU HD21   H N N 287 
LEU HD22   H N N 288 
LEU HD23   H N N 289 
LEU HXT    H N N 290 
LYS N      N N N 291 
LYS CA     C N S 292 
LYS C      C N N 293 
LYS O      O N N 294 
LYS CB     C N N 295 
LYS CG     C N N 296 
LYS CD     C N N 297 
LYS CE     C N N 298 
LYS NZ     N N N 299 
LYS OXT    O N N 300 
LYS H      H N N 301 
LYS H2     H N N 302 
LYS HA     H N N 303 
LYS HB2    H N N 304 
LYS HB3    H N N 305 
LYS HG2    H N N 306 
LYS HG3    H N N 307 
LYS HD2    H N N 308 
LYS HD3    H N N 309 
LYS HE2    H N N 310 
LYS HE3    H N N 311 
LYS HZ1    H N N 312 
LYS HZ2    H N N 313 
LYS HZ3    H N N 314 
LYS HXT    H N N 315 
MAN C1     C N S 316 
MAN C2     C N S 317 
MAN C3     C N S 318 
MAN C4     C N S 319 
MAN C5     C N R 320 
MAN C6     C N N 321 
MAN O1     O N N 322 
MAN O2     O N N 323 
MAN O3     O N N 324 
MAN O4     O N N 325 
MAN O5     O N N 326 
MAN O6     O N N 327 
MAN H1     H N N 328 
MAN H2     H N N 329 
MAN H3     H N N 330 
MAN H4     H N N 331 
MAN H5     H N N 332 
MAN H61    H N N 333 
MAN H62    H N N 334 
MAN HO1    H N N 335 
MAN HO2    H N N 336 
MAN HO3    H N N 337 
MAN HO4    H N N 338 
MAN HO6    H N N 339 
MET N      N N N 340 
MET CA     C N S 341 
MET C      C N N 342 
MET O      O N N 343 
MET CB     C N N 344 
MET CG     C N N 345 
MET SD     S N N 346 
MET CE     C N N 347 
MET OXT    O N N 348 
MET H      H N N 349 
MET H2     H N N 350 
MET HA     H N N 351 
MET HB2    H N N 352 
MET HB3    H N N 353 
MET HG2    H N N 354 
MET HG3    H N N 355 
MET HE1    H N N 356 
MET HE2    H N N 357 
MET HE3    H N N 358 
MET HXT    H N N 359 
NAG C1     C N R 360 
NAG C2     C N R 361 
NAG C3     C N R 362 
NAG C4     C N S 363 
NAG C5     C N R 364 
NAG C6     C N N 365 
NAG C7     C N N 366 
NAG C8     C N N 367 
NAG N2     N N N 368 
NAG O1     O N N 369 
NAG O3     O N N 370 
NAG O4     O N N 371 
NAG O5     O N N 372 
NAG O6     O N N 373 
NAG O7     O N N 374 
NAG H1     H N N 375 
NAG H2     H N N 376 
NAG H3     H N N 377 
NAG H4     H N N 378 
NAG H5     H N N 379 
NAG H61    H N N 380 
NAG H62    H N N 381 
NAG H81    H N N 382 
NAG H82    H N N 383 
NAG H83    H N N 384 
NAG HN2    H N N 385 
NAG HO1    H N N 386 
NAG HO3    H N N 387 
NAG HO4    H N N 388 
NAG HO6    H N N 389 
PHE N      N N N 390 
PHE CA     C N S 391 
PHE C      C N N 392 
PHE O      O N N 393 
PHE CB     C N N 394 
PHE CG     C Y N 395 
PHE CD1    C Y N 396 
PHE CD2    C Y N 397 
PHE CE1    C Y N 398 
PHE CE2    C Y N 399 
PHE CZ     C Y N 400 
PHE OXT    O N N 401 
PHE H      H N N 402 
PHE H2     H N N 403 
PHE HA     H N N 404 
PHE HB2    H N N 405 
PHE HB3    H N N 406 
PHE HD1    H N N 407 
PHE HD2    H N N 408 
PHE HE1    H N N 409 
PHE HE2    H N N 410 
PHE HZ     H N N 411 
PHE HXT    H N N 412 
PRO N      N N N 413 
PRO CA     C N S 414 
PRO C      C N N 415 
PRO O      O N N 416 
PRO CB     C N N 417 
PRO CG     C N N 418 
PRO CD     C N N 419 
PRO OXT    O N N 420 
PRO H      H N N 421 
PRO HA     H N N 422 
PRO HB2    H N N 423 
PRO HB3    H N N 424 
PRO HG2    H N N 425 
PRO HG3    H N N 426 
PRO HD2    H N N 427 
PRO HD3    H N N 428 
PRO HXT    H N N 429 
SCN S      S N N 430 
SCN C      C N N 431 
SCN N      N N N 432 
SER N      N N N 433 
SER CA     C N S 434 
SER C      C N N 435 
SER O      O N N 436 
SER CB     C N N 437 
SER OG     O N N 438 
SER OXT    O N N 439 
SER H      H N N 440 
SER H2     H N N 441 
SER HA     H N N 442 
SER HB2    H N N 443 
SER HB3    H N N 444 
SER HG     H N N 445 
SER HXT    H N N 446 
THR N      N N N 447 
THR CA     C N S 448 
THR C      C N N 449 
THR O      O N N 450 
THR CB     C N R 451 
THR OG1    O N N 452 
THR CG2    C N N 453 
THR OXT    O N N 454 
THR H      H N N 455 
THR H2     H N N 456 
THR HA     H N N 457 
THR HB     H N N 458 
THR HG1    H N N 459 
THR HG21   H N N 460 
THR HG22   H N N 461 
THR HG23   H N N 462 
THR HXT    H N N 463 
TRP N      N N N 464 
TRP CA     C N S 465 
TRP C      C N N 466 
TRP O      O N N 467 
TRP CB     C N N 468 
TRP CG     C Y N 469 
TRP CD1    C Y N 470 
TRP CD2    C Y N 471 
TRP NE1    N Y N 472 
TRP CE2    C Y N 473 
TRP CE3    C Y N 474 
TRP CZ2    C Y N 475 
TRP CZ3    C Y N 476 
TRP CH2    C Y N 477 
TRP OXT    O N N 478 
TRP H      H N N 479 
TRP H2     H N N 480 
TRP HA     H N N 481 
TRP HB2    H N N 482 
TRP HB3    H N N 483 
TRP HD1    H N N 484 
TRP HE1    H N N 485 
TRP HE3    H N N 486 
TRP HZ2    H N N 487 
TRP HZ3    H N N 488 
TRP HH2    H N N 489 
TRP HXT    H N N 490 
TYR N      N N N 491 
TYR CA     C N S 492 
TYR C      C N N 493 
TYR O      O N N 494 
TYR CB     C N N 495 
TYR CG     C Y N 496 
TYR CD1    C Y N 497 
TYR CD2    C Y N 498 
TYR CE1    C Y N 499 
TYR CE2    C Y N 500 
TYR CZ     C Y N 501 
TYR OH     O N N 502 
TYR OXT    O N N 503 
TYR H      H N N 504 
TYR H2     H N N 505 
TYR HA     H N N 506 
TYR HB2    H N N 507 
TYR HB3    H N N 508 
TYR HD1    H N N 509 
TYR HD2    H N N 510 
TYR HE1    H N N 511 
TYR HE2    H N N 512 
TYR HH     H N N 513 
TYR HXT    H N N 514 
VAL N      N N N 515 
VAL CA     C N S 516 
VAL C      C N N 517 
VAL O      O N N 518 
VAL CB     C N N 519 
VAL CG1    C N N 520 
VAL CG2    C N N 521 
VAL OXT    O N N 522 
VAL H      H N N 523 
VAL H2     H N N 524 
VAL HA     H N N 525 
VAL HB     H N N 526 
VAL HG11   H N N 527 
VAL HG12   H N N 528 
VAL HG13   H N N 529 
VAL HG21   H N N 530 
VAL HG22   H N N 531 
VAL HG23   H N N 532 
VAL HXT    H N N 533 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
HIS N     CA     sing N N 220 
HIS N     H      sing N N 221 
HIS N     H2     sing N N 222 
HIS CA    C      sing N N 223 
HIS CA    CB     sing N N 224 
HIS CA    HA     sing N N 225 
HIS C     O      doub N N 226 
HIS C     OXT    sing N N 227 
HIS CB    CG     sing N N 228 
HIS CB    HB2    sing N N 229 
HIS CB    HB3    sing N N 230 
HIS CG    ND1    sing Y N 231 
HIS CG    CD2    doub Y N 232 
HIS ND1   CE1    doub Y N 233 
HIS ND1   HD1    sing N N 234 
HIS CD2   NE2    sing Y N 235 
HIS CD2   HD2    sing N N 236 
HIS CE1   NE2    sing Y N 237 
HIS CE1   HE1    sing N N 238 
HIS NE2   HE2    sing N N 239 
HIS OXT   HXT    sing N N 240 
HOH O     H1     sing N N 241 
HOH O     H2     sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MAN C1    C2     sing N N 309 
MAN C1    O1     sing N N 310 
MAN C1    O5     sing N N 311 
MAN C1    H1     sing N N 312 
MAN C2    C3     sing N N 313 
MAN C2    O2     sing N N 314 
MAN C2    H2     sing N N 315 
MAN C3    C4     sing N N 316 
MAN C3    O3     sing N N 317 
MAN C3    H3     sing N N 318 
MAN C4    C5     sing N N 319 
MAN C4    O4     sing N N 320 
MAN C4    H4     sing N N 321 
MAN C5    C6     sing N N 322 
MAN C5    O5     sing N N 323 
MAN C5    H5     sing N N 324 
MAN C6    O6     sing N N 325 
MAN C6    H61    sing N N 326 
MAN C6    H62    sing N N 327 
MAN O1    HO1    sing N N 328 
MAN O2    HO2    sing N N 329 
MAN O3    HO3    sing N N 330 
MAN O4    HO4    sing N N 331 
MAN O6    HO6    sing N N 332 
MET N     CA     sing N N 333 
MET N     H      sing N N 334 
MET N     H2     sing N N 335 
MET CA    C      sing N N 336 
MET CA    CB     sing N N 337 
MET CA    HA     sing N N 338 
MET C     O      doub N N 339 
MET C     OXT    sing N N 340 
MET CB    CG     sing N N 341 
MET CB    HB2    sing N N 342 
MET CB    HB3    sing N N 343 
MET CG    SD     sing N N 344 
MET CG    HG2    sing N N 345 
MET CG    HG3    sing N N 346 
MET SD    CE     sing N N 347 
MET CE    HE1    sing N N 348 
MET CE    HE2    sing N N 349 
MET CE    HE3    sing N N 350 
MET OXT   HXT    sing N N 351 
NAG C1    C2     sing N N 352 
NAG C1    O1     sing N N 353 
NAG C1    O5     sing N N 354 
NAG C1    H1     sing N N 355 
NAG C2    C3     sing N N 356 
NAG C2    N2     sing N N 357 
NAG C2    H2     sing N N 358 
NAG C3    C4     sing N N 359 
NAG C3    O3     sing N N 360 
NAG C3    H3     sing N N 361 
NAG C4    C5     sing N N 362 
NAG C4    O4     sing N N 363 
NAG C4    H4     sing N N 364 
NAG C5    C6     sing N N 365 
NAG C5    O5     sing N N 366 
NAG C5    H5     sing N N 367 
NAG C6    O6     sing N N 368 
NAG C6    H61    sing N N 369 
NAG C6    H62    sing N N 370 
NAG C7    C8     sing N N 371 
NAG C7    N2     sing N N 372 
NAG C7    O7     doub N N 373 
NAG C8    H81    sing N N 374 
NAG C8    H82    sing N N 375 
NAG C8    H83    sing N N 376 
NAG N2    HN2    sing N N 377 
NAG O1    HO1    sing N N 378 
NAG O3    HO3    sing N N 379 
NAG O4    HO4    sing N N 380 
NAG O6    HO6    sing N N 381 
PHE N     CA     sing N N 382 
PHE N     H      sing N N 383 
PHE N     H2     sing N N 384 
PHE CA    C      sing N N 385 
PHE CA    CB     sing N N 386 
PHE CA    HA     sing N N 387 
PHE C     O      doub N N 388 
PHE C     OXT    sing N N 389 
PHE CB    CG     sing N N 390 
PHE CB    HB2    sing N N 391 
PHE CB    HB3    sing N N 392 
PHE CG    CD1    doub Y N 393 
PHE CG    CD2    sing Y N 394 
PHE CD1   CE1    sing Y N 395 
PHE CD1   HD1    sing N N 396 
PHE CD2   CE2    doub Y N 397 
PHE CD2   HD2    sing N N 398 
PHE CE1   CZ     doub Y N 399 
PHE CE1   HE1    sing N N 400 
PHE CE2   CZ     sing Y N 401 
PHE CE2   HE2    sing N N 402 
PHE CZ    HZ     sing N N 403 
PHE OXT   HXT    sing N N 404 
PRO N     CA     sing N N 405 
PRO N     CD     sing N N 406 
PRO N     H      sing N N 407 
PRO CA    C      sing N N 408 
PRO CA    CB     sing N N 409 
PRO CA    HA     sing N N 410 
PRO C     O      doub N N 411 
PRO C     OXT    sing N N 412 
PRO CB    CG     sing N N 413 
PRO CB    HB2    sing N N 414 
PRO CB    HB3    sing N N 415 
PRO CG    CD     sing N N 416 
PRO CG    HG2    sing N N 417 
PRO CG    HG3    sing N N 418 
PRO CD    HD2    sing N N 419 
PRO CD    HD3    sing N N 420 
PRO OXT   HXT    sing N N 421 
SCN S     C      sing N N 422 
SCN C     N      trip N N 423 
SER N     CA     sing N N 424 
SER N     H      sing N N 425 
SER N     H2     sing N N 426 
SER CA    C      sing N N 427 
SER CA    CB     sing N N 428 
SER CA    HA     sing N N 429 
SER C     O      doub N N 430 
SER C     OXT    sing N N 431 
SER CB    OG     sing N N 432 
SER CB    HB2    sing N N 433 
SER CB    HB3    sing N N 434 
SER OG    HG     sing N N 435 
SER OXT   HXT    sing N N 436 
THR N     CA     sing N N 437 
THR N     H      sing N N 438 
THR N     H2     sing N N 439 
THR CA    C      sing N N 440 
THR CA    CB     sing N N 441 
THR CA    HA     sing N N 442 
THR C     O      doub N N 443 
THR C     OXT    sing N N 444 
THR CB    OG1    sing N N 445 
THR CB    CG2    sing N N 446 
THR CB    HB     sing N N 447 
THR OG1   HG1    sing N N 448 
THR CG2   HG21   sing N N 449 
THR CG2   HG22   sing N N 450 
THR CG2   HG23   sing N N 451 
THR OXT   HXT    sing N N 452 
TRP N     CA     sing N N 453 
TRP N     H      sing N N 454 
TRP N     H2     sing N N 455 
TRP CA    C      sing N N 456 
TRP CA    CB     sing N N 457 
TRP CA    HA     sing N N 458 
TRP C     O      doub N N 459 
TRP C     OXT    sing N N 460 
TRP CB    CG     sing N N 461 
TRP CB    HB2    sing N N 462 
TRP CB    HB3    sing N N 463 
TRP CG    CD1    doub Y N 464 
TRP CG    CD2    sing Y N 465 
TRP CD1   NE1    sing Y N 466 
TRP CD1   HD1    sing N N 467 
TRP CD2   CE2    doub Y N 468 
TRP CD2   CE3    sing Y N 469 
TRP NE1   CE2    sing Y N 470 
TRP NE1   HE1    sing N N 471 
TRP CE2   CZ2    sing Y N 472 
TRP CE3   CZ3    doub Y N 473 
TRP CE3   HE3    sing N N 474 
TRP CZ2   CH2    doub Y N 475 
TRP CZ2   HZ2    sing N N 476 
TRP CZ3   CH2    sing Y N 477 
TRP CZ3   HZ3    sing N N 478 
TRP CH2   HH2    sing N N 479 
TRP OXT   HXT    sing N N 480 
TYR N     CA     sing N N 481 
TYR N     H      sing N N 482 
TYR N     H2     sing N N 483 
TYR CA    C      sing N N 484 
TYR CA    CB     sing N N 485 
TYR CA    HA     sing N N 486 
TYR C     O      doub N N 487 
TYR C     OXT    sing N N 488 
TYR CB    CG     sing N N 489 
TYR CB    HB2    sing N N 490 
TYR CB    HB3    sing N N 491 
TYR CG    CD1    doub Y N 492 
TYR CG    CD2    sing Y N 493 
TYR CD1   CE1    sing Y N 494 
TYR CD1   HD1    sing N N 495 
TYR CD2   CE2    doub Y N 496 
TYR CD2   HD2    sing N N 497 
TYR CE1   CZ     doub Y N 498 
TYR CE1   HE1    sing N N 499 
TYR CE2   CZ     sing Y N 500 
TYR CE2   HE2    sing N N 501 
TYR CZ    OH     sing N N 502 
TYR OH    HH     sing N N 503 
TYR OXT   HXT    sing N N 504 
VAL N     CA     sing N N 505 
VAL N     H      sing N N 506 
VAL N     H2     sing N N 507 
VAL CA    C      sing N N 508 
VAL CA    CB     sing N N 509 
VAL CA    HA     sing N N 510 
VAL C     O      doub N N 511 
VAL C     OXT    sing N N 512 
VAL CB    CG1    sing N N 513 
VAL CB    CG2    sing N N 514 
VAL CB    HB     sing N N 515 
VAL CG1   HG11   sing N N 516 
VAL CG1   HG12   sing N N 517 
VAL CG1   HG13   sing N N 518 
VAL CG2   HG21   sing N N 519 
VAL CG2   HG22   sing N N 520 
VAL CG2   HG23   sing N N 521 
VAL OXT   HXT    sing N N 522 
# 
_pdbx_audit_support.funding_organization   'European Cooperation in Science and Technology (COST) action' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           'COZYME (CA21162)' 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 NAG 2 n 
2 MAN 3 n 
2 MAN 4 n 
3 NAG 1 n 
3 NAG 2 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9H92 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.015357 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008642 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.007277 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . SER A 1 5   ? -48.369 -37.197 28.720  1.00 39.14 ? 5    SER A N     1 
ATOM   2    C CA    . SER A 1 5   ? -49.167 -35.999 28.373  1.00 36.03 ? 5    SER A CA    1 
ATOM   3    C C     . SER A 1 5   ? -49.537 -36.094 26.897  1.00 34.59 ? 5    SER A C     1 
ATOM   4    O O     . SER A 1 5   ? -48.922 -36.870 26.162  1.00 34.70 ? 5    SER A O     1 
ATOM   5    C CB    . SER A 1 5   ? -48.406 -34.717 28.693  1.00 38.12 ? 5    SER A CB    1 
ATOM   6    O OG    . SER A 1 5   ? -47.226 -34.566 27.906  1.00 33.48 ? 5    SER A OG    1 
ATOM   7    N N     . ALA A 1 6   ? -50.547 -35.316 26.491  1.00 30.06 ? 6    ALA A N     1 
ATOM   8    C CA    . ALA A 1 6   ? -50.878 -35.169 25.084  1.00 30.54 ? 6    ALA A CA    1 
ATOM   9    C C     . ALA A 1 6   ? -49.638 -34.702 24.316  1.00 25.77 ? 6    ALA A C     1 
ATOM   10   O O     . ALA A 1 6   ? -49.364 -35.192 23.221  1.00 23.72 ? 6    ALA A O     1 
ATOM   11   C CB    . ALA A 1 6   ? -51.995 -34.175 24.918  1.00 31.88 ? 6    ALA A CB    1 
ATOM   12   N N     . PHE A 1 7   ? -48.937 -33.709 24.886  1.00 23.20 ? 7    PHE A N     1 
ATOM   13   C CA    . PHE A 1 7   ? -47.716 -33.166 24.279  1.00 20.53 ? 7    PHE A CA    1 
ATOM   14   C C     . PHE A 1 7   ? -46.688 -34.266 24.021  1.00 19.21 ? 7    PHE A C     1 
ATOM   15   O O     . PHE A 1 7   ? -46.078 -34.327 22.949  1.00 18.09 ? 7    PHE A O     1 
ATOM   16   C CB    . PHE A 1 7   ? -47.136 -32.068 25.168  1.00 19.42 ? 7    PHE A CB    1 
ATOM   17   C CG    . PHE A 1 7   ? -45.861 -31.404 24.650  1.00 18.20 ? 7    PHE A CG    1 
ATOM   18   C CD1   . PHE A 1 7   ? -45.796 -30.859 23.379  1.00 17.94 ? 7    PHE A CD1   1 
ATOM   19   C CD2   . PHE A 1 7   ? -44.719 -31.349 25.444  1.00 18.26 ? 7    PHE A CD2   1 
ATOM   20   C CE1   . PHE A 1 7   ? -44.632 -30.242 22.934  1.00 18.30 ? 7    PHE A CE1   1 
ATOM   21   C CE2   . PHE A 1 7   ? -43.569 -30.710 25.012  1.00 19.02 ? 7    PHE A CE2   1 
ATOM   22   C CZ    . PHE A 1 7   ? -43.525 -30.155 23.754  1.00 19.37 ? 7    PHE A CZ    1 
ATOM   23   N N     . ALA A 1 8   ? -46.396 -35.085 25.027  1.00 19.60 ? 8    ALA A N     1 
ATOM   24   C CA    . ALA A 1 8   ? -45.422 -36.147 24.894  1.00 18.44 ? 8    ALA A CA    1 
ATOM   25   C C     . ALA A 1 8   ? -45.828 -37.163 23.823  1.00 17.27 ? 8    ALA A C     1 
ATOM   26   O O     . ALA A 1 8   ? -44.966 -37.644 23.078  1.00 17.98 ? 8    ALA A O     1 
ATOM   27   C CB    . ALA A 1 8   ? -45.228 -36.848 26.227  1.00 19.53 ? 8    ALA A CB    1 
ATOM   28   N N     . THR A 1 9   ? -47.114 -37.566 23.818  1.00 18.04 ? 9    THR A N     1 
ATOM   29   C CA    . THR A 1 9   ? -47.635 -38.514 22.847  1.00 18.21 ? 9    THR A CA    1 
ATOM   30   C C     . THR A 1 9   ? -47.455 -37.930 21.436  1.00 15.70 ? 9    THR A C     1 
ATOM   31   O O     . THR A 1 9   ? -47.047 -38.610 20.501  1.00 18.59 ? 9    THR A O     1 
ATOM   32   C CB    . THR A 1 9   ? -49.113 -38.745 23.197  1.00 22.29 ? 9    THR A CB    1 
ATOM   33   O OG1   . THR A 1 9   ? -49.090 -39.441 24.448  1.00 24.14 ? 9    THR A OG1   1 
ATOM   34   C CG2   . THR A 1 9   ? -49.871 -39.511 22.136  1.00 23.22 ? 9    THR A CG2   1 
ATOM   35   N N     . CYS A 1 10  ? -47.847 -36.690 21.302  1.00 16.12 ? 10   CYS A N     1 
ATOM   36   C CA    . CYS A 1 10  ? -47.842 -36.012 20.008  1.00 16.75 ? 10   CYS A CA    1 
ATOM   37   C C     . CYS A 1 10  ? -46.405 -35.921 19.500  1.00 14.91 ? 10   CYS A C     1 
ATOM   38   O O     . CYS A 1 10  ? -46.131 -36.220 18.354  1.00 15.88 ? 10   CYS A O     1 
ATOM   39   C CB    . CYS A 1 10  ? -48.541 -34.666 20.110  1.00 19.10 ? 10   CYS A CB    1 
ATOM   40   S SG    . CYS A 1 10  ? -48.614 -33.775 18.535  1.00 25.04 ? 10   CYS A SG    1 
ATOM   41   N N     . LEU A 1 11  ? -45.638 -35.807 20.449  1.00 15.23 ? 11   LEU A N     1 
ATOM   42   C CA    . LEU A 1 11  ? -44.322 -35.391 19.985  1.00 15.16 ? 11   LEU A CA    1 
ATOM   43   C C     . LEU A 1 11  ? -43.469 -36.603 19.617  1.00 14.52 ? 11   LEU A C     1 
ATOM   44   O O     . LEU A 1 11  ? -42.737 -36.611 18.631  1.00 15.53 ? 11   LEU A O     1 
ATOM   45   C CB    . LEU A 1 11  ? -43.699 -34.545 21.090  1.00 17.29 ? 11   LEU A CB    1 
ATOM   46   C CG    . LEU A 1 11  ? -42.281 -34.046 20.868  1.00 23.69 ? 11   LEU A CG    1 
ATOM   47   C CD1   . LEU A 1 11  ? -42.060 -33.097 19.691  1.00 19.78 ? 11   LEU A CD1   1 
ATOM   48   C CD2   . LEU A 1 11  ? -41.909 -33.356 22.195  1.00 24.72 ? 11   LEU A CD2   1 
ATOM   49   N N     . LEU A 1 12  ? -43.727 -37.772 20.305  1.00 13.88 ? 12   LEU A N     1 
ATOM   50   C CA    . LEU A 1 12  ? -43.265 -39.079 19.902  1.00 14.00 ? 12   LEU A CA    1 
ATOM   51   C C     . LEU A 1 12  ? -43.786 -39.444 18.509  1.00 14.49 ? 12   LEU A C     1 
ATOM   52   O O     . LEU A 1 12  ? -43.061 -39.982 17.661  1.00 14.83 ? 12   LEU A O     1 
ATOM   53   C CB    . LEU A 1 12  ? -43.666 -40.094 20.963  1.00 15.53 ? 12   LEU A CB    1 
ATOM   54   C CG    . LEU A 1 12  ? -43.223 -41.523 20.672  1.00 18.13 ? 12   LEU A CG    1 
ATOM   55   C CD1   . LEU A 1 12  ? -41.709 -41.639 20.643  1.00 18.97 ? 12   LEU A CD1   1 
ATOM   56   C CD2   . LEU A 1 12  ? -43.797 -42.458 21.742  1.00 20.21 ? 12   LEU A CD2   1 
ATOM   57   N N     . ALA A 1 13  ? -45.076 -39.184 18.249  1.00 14.59 ? 13   ALA A N     1 
ATOM   58   C CA    . ALA A 1 13  ? -45.609 -39.449 16.927  1.00 15.20 ? 13   ALA A CA    1 
ATOM   59   C C     . ALA A 1 13  ? -44.958 -38.543 15.866  1.00 15.57 ? 13   ALA A C     1 
ATOM   60   O O     . ALA A 1 13  ? -44.823 -38.978 14.724  1.00 15.42 ? 13   ALA A O     1 
ATOM   61   C CB    . ALA A 1 13  ? -47.125 -39.290 16.920  1.00 15.84 ? 13   ALA A CB    1 
ATOM   62   N N     . SER A 1 14  ? -44.605 -37.284 16.225  1.00 15.38 ? 14   SER A N     1 
ATOM   63   C CA    . SER A 1 14  ? -43.963 -36.386 15.263  1.00 15.82 ? 14   SER A CA    1 
ATOM   64   C C     . SER A 1 14  ? -42.669 -36.983 14.701  1.00 16.50 ? 14   SER A C     1 
ATOM   65   O O     . SER A 1 14  ? -42.307 -36.687 13.565  1.00 16.40 ? 14   SER A O     1 
ATOM   66   C CB    . SER A 1 14  ? -43.721 -34.984 15.821  1.00 15.56 ? 14   SER A CB    1 
ATOM   67   O OG    . SER A 1 14  ? -42.530 -34.912 16.616  1.00 15.42 ? 14   SER A OG    1 
ATOM   68   N N     . VAL A 1 15  ? -41.973 -37.853 15.463  1.00 14.24 ? 15   VAL A N     1 
ATOM   69   C CA    . VAL A 1 15  ? -40.777 -38.525 14.992  1.00 14.39 ? 15   VAL A CA    1 
ATOM   70   C C     . VAL A 1 15  ? -41.042 -40.008 14.718  1.00 15.11 ? 15   VAL A C     1 
ATOM   71   O O     . VAL A 1 15  ? -40.141 -40.816 14.760  1.00 15.68 ? 15   VAL A O     1 
ATOM   72   C CB    . VAL A 1 15  ? -39.610 -38.350 15.988  1.00 15.53 ? 15   VAL A CB    1 
ATOM   73   C CG1   . VAL A 1 15  ? -39.203 -36.882 16.049  1.00 16.68 ? 15   VAL A CG1   1 
ATOM   74   C CG2   . VAL A 1 15  ? -39.928 -38.890 17.383  1.00 14.79 ? 15   VAL A CG2   1 
ATOM   75   N N     . GLY A 1 16  ? -42.297 -40.369 14.419  1.00 16.88 ? 16   GLY A N     1 
ATOM   76   C CA    . GLY A 1 16  ? -42.591 -41.708 13.919  1.00 17.34 ? 16   GLY A CA    1 
ATOM   77   C C     . GLY A 1 16  ? -42.427 -42.805 14.965  1.00 18.47 ? 16   GLY A C     1 
ATOM   78   O O     . GLY A 1 16  ? -42.163 -43.944 14.612  1.00 18.53 ? 16   GLY A O     1 
ATOM   79   N N     . GLY A 1 17  ? -42.554 -42.454 16.243  1.00 17.68 ? 17   GLY A N     1 
ATOM   80   C CA    . GLY A 1 17  ? -42.465 -43.444 17.313  1.00 18.72 ? 17   GLY A CA    1 
ATOM   81   C C     . GLY A 1 17  ? -41.021 -43.790 17.685  1.00 17.74 ? 17   GLY A C     1 
ATOM   82   O O     . GLY A 1 17  ? -40.768 -44.713 18.464  1.00 16.76 ? 17   GLY A O     1 
ATOM   83   N N     . ASN A 1 18  ? -40.052 -43.064 17.126  1.00 16.22 ? 18   ASN A N     1 
ATOM   84   C CA    . ASN A 1 18  ? -38.668 -43.307 17.491  1.00 16.09 ? 18   ASN A CA    1 
ATOM   85   C C     . ASN A 1 18  ? -38.374 -42.631 18.834  1.00 16.25 ? 18   ASN A C     1 
ATOM   86   O O     . ASN A 1 18  ? -38.127 -41.435 18.864  1.00 14.22 ? 18   ASN A O     1 
ATOM   87   C CB    . ASN A 1 18  ? -37.736 -42.814 16.400  1.00 16.68 ? 18   ASN A CB    1 
ATOM   88   C CG    . ASN A 1 18  ? -36.274 -43.002 16.706  1.00 16.62 ? 18   ASN A CG    1 
ATOM   89   O OD1   . ASN A 1 18  ? -35.879 -43.545 17.734  1.00 16.15 ? 18   ASN A OD1   1 
ATOM   90   N ND2   . ASN A 1 18  ? -35.445 -42.593 15.766  1.00 19.87 ? 18   ASN A ND2   1 
ATOM   91   N N     . SER A 1 19  ? -38.361 -43.405 19.927  1.00 15.46 ? 19   SER A N     1 
ATOM   92   C CA    . SER A 1 19  ? -38.215 -42.857 21.273  1.00 15.96 ? 19   SER A CA    1 
ATOM   93   C C     . SER A 1 19  ? -36.816 -42.275 21.515  1.00 15.96 ? 19   SER A C     1 
ATOM   94   O O     . SER A 1 19  ? -36.674 -41.497 22.449  1.00 17.21 ? 19   SER A O     1 
ATOM   95   C CB    . SER A 1 19  ? -38.576 -43.868 22.355  1.00 15.22 ? 19   SER A CB    1 
ATOM   96   O OG    . SER A 1 19  ? -37.659 -44.936 22.351  1.00 17.79 ? 19   SER A OG    1 
ATOM   97   N N     . SER A 1 20  ? -35.837 -42.606 20.679  1.00 15.82 ? 20   SER A N     1 
ATOM   98   C CA    . SER A 1 20  ? -34.498 -42.031 20.680  1.00 16.79 ? 20   SER A CA    1 
ATOM   99   C C     . SER A 1 20  ? -34.480 -40.634 20.066  1.00 15.65 ? 20   SER A C     1 
ATOM   100  O O     . SER A 1 20  ? -33.453 -39.967 20.158  1.00 15.25 ? 20   SER A O     1 
ATOM   101  C CB    . SER A 1 20  ? -33.502 -42.886 19.919  1.00 20.42 ? 20   SER A CB    1 
ATOM   102  O OG    . SER A 1 20  ? -33.309 -44.114 20.587  1.00 26.27 ? 20   SER A OG    1 
ATOM   103  N N     . ALA A 1 21  ? -35.574 -40.211 19.428  1.00 13.47 ? 21   ALA A N     1 
ATOM   104  C CA    . ALA A 1 21  ? -35.591 -38.921 18.742  1.00 14.39 ? 21   ALA A CA    1 
ATOM   105  C C     . ALA A 1 21  ? -36.402 -37.869 19.512  1.00 13.21 ? 21   ALA A C     1 
ATOM   106  O O     . ALA A 1 21  ? -36.734 -36.791 18.987  1.00 12.63 ? 21   ALA A O     1 
ATOM   107  C CB    . ALA A 1 21  ? -36.081 -39.093 17.331  1.00 15.26 ? 21   ALA A CB    1 
ATOM   108  N N     . VAL A 1 22  ? -36.784 -38.217 20.751  1.00 13.22 ? 22   VAL A N     1 
ATOM   109  C CA    . VAL A 1 22  ? -37.411 -37.307 21.683  1.00 12.86 ? 22   VAL A CA    1 
ATOM   110  C C     . VAL A 1 22  ? -36.792 -37.535 23.057  1.00 13.15 ? 22   VAL A C     1 
ATOM   111  O O     . VAL A 1 22  ? -36.433 -38.675 23.411  1.00 13.58 ? 22   VAL A O     1 
ATOM   112  C CB    . VAL A 1 22  ? -38.934 -37.427 21.800  1.00 16.11 ? 22   VAL A CB    1 
ATOM   113  C CG1   . VAL A 1 22  ? -39.598 -36.816 20.600  1.00 20.14 ? 22   VAL A CG1   1 
ATOM   114  C CG2   . VAL A 1 22  ? -39.370 -38.873 22.044  1.00 15.45 ? 22   VAL A CG2   1 
ATOM   115  N N     . ALA A 1 23  ? -36.699 -36.432 23.823  1.00 12.83 ? 23   ALA A N     1 
ATOM   116  C CA    . ALA A 1 23  ? -36.304 -36.518 25.223  1.00 14.12 ? 23   ALA A CA    1 
ATOM   117  C C     . ALA A 1 23  ? -37.147 -35.574 26.065  1.00 13.97 ? 23   ALA A C     1 
ATOM   118  O O     . ALA A 1 23  ? -37.461 -34.477 25.624  1.00 12.60 ? 23   ALA A O     1 
ATOM   119  C CB    . ALA A 1 23  ? -34.846 -36.214 25.397  1.00 14.93 ? 23   ALA A CB    1 
ATOM   120  N N     . PHE A 1 24  ? -37.484 -36.027 27.279  1.00 13.98 ? 24   PHE A N     1 
ATOM   121  C CA    . PHE A 1 24  ? -38.270 -35.230 28.213  1.00 14.38 ? 24   PHE A CA    1 
ATOM   122  C C     . PHE A 1 24  ? -37.529 -35.049 29.539  1.00 13.82 ? 24   PHE A C     1 
ATOM   123  O O     . PHE A 1 24  ? -36.684 -35.864 29.883  1.00 15.17 ? 24   PHE A O     1 
ATOM   124  C CB    . PHE A 1 24  ? -39.616 -35.909 28.460  1.00 14.69 ? 24   PHE A CB    1 
ATOM   125  C CG    . PHE A 1 24  ? -40.409 -36.073 27.179  1.00 16.97 ? 24   PHE A CG    1 
ATOM   126  C CD1   . PHE A 1 24  ? -41.140 -35.014 26.673  1.00 19.07 ? 24   PHE A CD1   1 
ATOM   127  C CD2   . PHE A 1 24  ? -40.319 -37.246 26.445  1.00 17.33 ? 24   PHE A CD2   1 
ATOM   128  C CE1   . PHE A 1 24  ? -41.813 -35.144 25.458  1.00 21.08 ? 24   PHE A CE1   1 
ATOM   129  C CE2   . PHE A 1 24  ? -41.021 -37.386 25.254  1.00 20.51 ? 24   PHE A CE2   1 
ATOM   130  C CZ    . PHE A 1 24  ? -41.747 -36.339 24.758  1.00 18.41 ? 24   PHE A CZ    1 
ATOM   131  N N     . PRO A 1 25  ? -37.848 -33.969 30.296  1.00 15.13 ? 25   PRO A N     1 
ATOM   132  C CA    . PRO A 1 25  ? -37.254 -33.727 31.604  1.00 16.78 ? 25   PRO A CA    1 
ATOM   133  C C     . PRO A 1 25  ? -37.531 -35.009 32.409  1.00 19.16 ? 25   PRO A C     1 
ATOM   134  O O     . PRO A 1 25  ? -38.521 -35.704 32.213  1.00 25.47 ? 25   PRO A O     1 
ATOM   135  C CB    . PRO A 1 25  ? -38.028 -32.536 32.149  1.00 17.05 ? 25   PRO A CB    1 
ATOM   136  C CG    . PRO A 1 25  ? -38.523 -31.784 30.908  1.00 16.31 ? 25   PRO A CG    1 
ATOM   137  C CD    . PRO A 1 25  ? -38.804 -32.917 29.926  1.00 16.24 ? 25   PRO A CD    1 
ATOM   138  N N     . ASN A 1 26  ? -36.620 -35.351 33.264  1.00 24.28 ? 26   ASN A N     1 
ATOM   139  C CA    . ASN A 1 26  ? -36.793 -36.553 34.065  1.00 19.36 ? 26   ASN A CA    1 
ATOM   140  C C     . ASN A 1 26  ? -36.328 -37.787 33.313  1.00 16.38 ? 26   ASN A C     1 
ATOM   141  O O     . ASN A 1 26  ? -36.458 -38.850 33.893  1.00 16.88 ? 26   ASN A O     1 
ATOM   142  C CB    . ASN A 1 26  ? -38.214 -36.936 34.510  1.00 21.03 ? 26   ASN A CB    1 
ATOM   143  C CG    . ASN A 1 26  ? -38.835 -35.915 35.431  1.00 21.84 ? 26   ASN A CG    1 
ATOM   144  O OD1   . ASN A 1 26  ? -39.987 -35.530 35.208  1.00 33.92 ? 26   ASN A OD1   1 
ATOM   145  N ND2   . ASN A 1 26  ? -38.068 -35.359 36.356  1.00 18.67 ? 26   ASN A ND2   1 
ATOM   146  N N     . GLN A 1 27  ? -35.837 -37.678 32.074  1.00 15.66 ? 27   GLN A N     1 
ATOM   147  C CA    . GLN A 1 27  ? -35.151 -38.810 31.467  1.00 15.80 ? 27   GLN A CA    1 
ATOM   148  C C     . GLN A 1 27  ? -33.732 -38.689 32.018  1.00 15.02 ? 27   GLN A C     1 
ATOM   149  O O     . GLN A 1 27  ? -33.217 -37.588 32.212  1.00 14.37 ? 27   GLN A O     1 
ATOM   150  C CB    . GLN A 1 27  ? -34.970 -38.751 29.948  1.00 18.72 ? 27   GLN A CB    1 
ATOM   151  C CG    . GLN A 1 27  ? -36.069 -39.447 29.179  1.00 26.56 ? 27   GLN A CG    1 
ATOM   152  C CD    . GLN A 1 27  ? -35.872 -39.322 27.682  1.00 20.92 ? 27   GLN A CD    1 
ATOM   153  O OE1   . GLN A 1 27  ? -34.766 -39.519 27.152  1.00 26.51 ? 27   GLN A OE1   1 
ATOM   154  N NE2   . GLN A 1 27  ? -36.994 -39.080 27.049  1.00 26.15 ? 27   GLN A NE2   1 
ATOM   155  N N     . ALA A 1 28  ? -33.084 -39.835 32.245  1.00 13.69 ? 28   ALA A N     1 
ATOM   156  C CA    . ALA A 1 28  ? -31.660 -39.845 32.522  1.00 15.90 ? 28   ALA A CA    1 
ATOM   157  C C     . ALA A 1 28  ? -30.914 -39.053 31.456  1.00 15.68 ? 28   ALA A C     1 
ATOM   158  O O     . ALA A 1 28  ? -31.239 -39.091 30.260  1.00 14.37 ? 28   ALA A O     1 
ATOM   159  C CB    . ALA A 1 28  ? -31.135 -41.260 32.556  1.00 18.28 ? 28   ALA A CB    1 
ATOM   160  N N     . ASN A 1 29  ? -29.910 -38.305 31.919  1.00 15.75 ? 29   ASN A N     1 
ATOM   161  C CA    . ASN A 1 29  ? -29.007 -37.590 31.036  1.00 15.70 ? 29   ASN A CA    1 
ATOM   162  C C     . ASN A 1 29  ? -29.640 -36.368 30.380  1.00 13.24 ? 29   ASN A C     1 
ATOM   163  O O     . ASN A 1 29  ? -29.046 -35.817 29.467  1.00 13.67 ? 29   ASN A O     1 
ATOM   164  C CB    . ASN A 1 29  ? -28.404 -38.480 29.961  1.00 17.49 ? 29   ASN A CB    1 
ATOM   165  C CG    . ASN A 1 29  ? -27.378 -39.435 30.511  1.00 25.11 ? 29   ASN A CG    1 
ATOM   166  O OD1   . ASN A 1 29  ? -26.867 -39.236 31.610  1.00 20.35 ? 29   ASN A OD1   1 
ATOM   167  N ND2   . ASN A 1 29  ? -27.107 -40.492 29.749  1.00 33.73 ? 29   ASN A ND2   1 
ATOM   168  N N     . TYR A 1 30  ? -30.814 -35.925 30.844  1.00 12.29 ? 30   TYR A N     1 
ATOM   169  C CA    . TYR A 1 30  ? -31.479 -34.829 30.155  1.00 12.12 ? 30   TYR A CA    1 
ATOM   170  C C     . TYR A 1 30  ? -30.607 -33.582 30.125  1.00 13.37 ? 30   TYR A C     1 
ATOM   171  O O     . TYR A 1 30  ? -30.474 -32.925 29.083  1.00 13.05 ? 30   TYR A O     1 
ATOM   172  C CB    . TYR A 1 30  ? -32.837 -34.492 30.795  1.00 12.40 ? 30   TYR A CB    1 
ATOM   173  C CG    . TYR A 1 30  ? -33.700 -33.549 29.963  1.00 11.93 ? 30   TYR A CG    1 
ATOM   174  C CD1   . TYR A 1 30  ? -34.286 -33.995 28.784  1.00 12.22 ? 30   TYR A CD1   1 
ATOM   175  C CD2   . TYR A 1 30  ? -34.010 -32.258 30.392  1.00 12.50 ? 30   TYR A CD2   1 
ATOM   176  C CE1   . TYR A 1 30  ? -35.121 -33.184 28.044  1.00 12.65 ? 30   TYR A CE1   1 
ATOM   177  C CE2   . TYR A 1 30  ? -34.822 -31.419 29.634  1.00 11.42 ? 30   TYR A CE2   1 
ATOM   178  C CZ    . TYR A 1 30  ? -35.396 -31.902 28.468  1.00 13.17 ? 30   TYR A CZ    1 
ATOM   179  O OH    . TYR A 1 30  ? -36.270 -31.175 27.715  1.00 12.69 ? 30   TYR A OH    1 
ATOM   180  N N     . SER A 1 31  ? -29.989 -33.229 31.265  1.00 15.45 ? 31   SER A N     1 
ATOM   181  C CA    . SER A 1 31  ? -29.223 -32.002 31.267  1.00 16.52 ? 31   SER A CA    1 
ATOM   182  C C     . SER A 1 31  ? -28.024 -32.068 30.310  1.00 14.26 ? 31   SER A C     1 
ATOM   183  O O     . SER A 1 31  ? -27.673 -31.039 29.733  1.00 15.29 ? 31   SER A O     1 
ATOM   184  C CB    . SER A 1 31  ? -28.849 -31.599 32.695  1.00 20.45 ? 31   SER A CB    1 
ATOM   185  O OG    . SER A 1 31  ? -28.040 -32.593 33.264  1.00 22.27 ? 31   SER A OG    1 
ATOM   186  N N     . THR A 1 32  ? -27.462 -33.255 30.033  1.00 13.45 ? 32   THR A N     1 
ATOM   187  C CA    . THR A 1 32  ? -26.407 -33.428 29.035  1.00 14.05 ? 32   THR A CA    1 
ATOM   188  C C     . THR A 1 32  ? -27.015 -33.348 27.634  1.00 13.30 ? 32   THR A C     1 
ATOM   189  O O     . THR A 1 32  ? -26.444 -32.727 26.751  1.00 13.46 ? 32   THR A O     1 
ATOM   190  C CB    . THR A 1 32  ? -25.678 -34.763 29.238  1.00 17.45 ? 32   THR A CB    1 
ATOM   191  O OG1   . THR A 1 32  ? -25.027 -34.652 30.508  1.00 20.18 ? 32   THR A OG1   1 
ATOM   192  C CG2   . THR A 1 32  ? -24.618 -35.047 28.196  1.00 18.57 ? 32   THR A CG2   1 
ATOM   193  N N     . LEU A 1 33  ? -28.168 -33.967 27.403  1.00 12.55 ? 33   LEU A N     1 
ATOM   194  C CA    . LEU A 1 33  ? -28.819 -33.898 26.092  1.00 12.59 ? 33   LEU A CA    1 
ATOM   195  C C     . LEU A 1 33  ? -29.145 -32.458 25.685  1.00 13.05 ? 33   LEU A C     1 
ATOM   196  O O     . LEU A 1 33  ? -29.087 -32.125 24.500  1.00 13.49 ? 33   LEU A O     1 
ATOM   197  C CB    . LEU A 1 33  ? -30.071 -34.765 26.082  1.00 12.87 ? 33   LEU A CB    1 
ATOM   198  C CG    . LEU A 1 33  ? -29.819 -36.271 26.129  1.00 14.51 ? 33   LEU A CG    1 
ATOM   199  C CD1   . LEU A 1 33  ? -31.070 -37.056 26.383  1.00 15.60 ? 33   LEU A CD1   1 
ATOM   200  C CD2   . LEU A 1 33  ? -29.221 -36.735 24.840  1.00 14.94 ? 33   LEU A CD2   1 
ATOM   201  N N     . VAL A 1 34  ? -29.521 -31.603 26.657  1.00 12.73 ? 34   VAL A N     1 
ATOM   202  C CA    . VAL A 1 34  ? -29.754 -30.190 26.395  1.00 12.89 ? 34   VAL A CA    1 
ATOM   203  C C     . VAL A 1 34  ? -28.504 -29.514 25.818  1.00 13.08 ? 34   VAL A C     1 
ATOM   204  O O     . VAL A 1 34  ? -28.636 -28.611 24.972  1.00 12.42 ? 34   VAL A O     1 
ATOM   205  C CB    . VAL A 1 34  ? -30.268 -29.495 27.668  1.00 12.60 ? 34   VAL A CB    1 
ATOM   206  C CG1   . VAL A 1 34  ? -30.286 -27.966 27.565  1.00 14.01 ? 34   VAL A CG1   1 
ATOM   207  C CG2   . VAL A 1 34  ? -31.629 -30.034 28.073  1.00 13.55 ? 34   VAL A CG2   1 
ATOM   208  N N     . ALA A 1 35  ? -27.314 -29.956 26.267  1.00 12.78 ? 35   ALA A N     1 
ATOM   209  C CA    . ALA A 1 35  ? -26.042 -29.555 25.670  1.00 14.23 ? 35   ALA A CA    1 
ATOM   210  C C     . ALA A 1 35  ? -25.853 -28.047 25.763  1.00 12.85 ? 35   ALA A C     1 
ATOM   211  O O     . ALA A 1 35  ? -25.718 -27.343 24.749  1.00 14.17 ? 35   ALA A O     1 
ATOM   212  C CB    . ALA A 1 35  ? -25.935 -30.042 24.247  1.00 14.16 ? 35   ALA A CB    1 
ATOM   213  N N     . PRO A 1 36  ? -25.762 -27.482 26.988  1.00 12.32 ? 36   PRO A N     1 
ATOM   214  C CA    . PRO A 1 36  ? -25.534 -26.045 27.124  1.00 12.35 ? 36   PRO A CA    1 
ATOM   215  C C     . PRO A 1 36  ? -24.187 -25.629 26.539  1.00 12.26 ? 36   PRO A C     1 
ATOM   216  O O     . PRO A 1 36  ? -23.207 -26.378 26.615  1.00 14.34 ? 36   PRO A O     1 
ATOM   217  C CB    . PRO A 1 36  ? -25.572 -25.853 28.647  1.00 12.57 ? 36   PRO A CB    1 
ATOM   218  C CG    . PRO A 1 36  ? -25.168 -27.172 29.221  1.00 13.09 ? 36   PRO A CG    1 
ATOM   219  C CD    . PRO A 1 36  ? -25.840 -28.163 28.283  1.00 13.05 ? 36   PRO A CD    1 
ATOM   220  N N     . TYR A 1 37  ? -24.183 -24.424 25.947  1.00 12.02 ? 37   TYR A N     1 
ATOM   221  C CA    . TYR A 1 37  ? -22.944 -23.789 25.529  1.00 12.18 ? 37   TYR A CA    1 
ATOM   222  C C     . TYR A 1 37  ? -22.460 -22.905 26.679  1.00 12.07 ? 37   TYR A C     1 
ATOM   223  O O     . TYR A 1 37  ? -21.334 -23.035 27.147  1.00 12.22 ? 37   TYR A O     1 
ATOM   224  C CB    . TYR A 1 37  ? -23.156 -23.014 24.226  1.00 12.14 ? 37   TYR A CB    1 
ATOM   225  C CG    . TYR A 1 37  ? -21.813 -22.518 23.734  1.00 12.22 ? 37   TYR A CG    1 
ATOM   226  C CD1   . TYR A 1 37  ? -21.046 -23.325 22.915  1.00 13.91 ? 37   TYR A CD1   1 
ATOM   227  C CD2   . TYR A 1 37  ? -21.290 -21.311 24.157  1.00 13.46 ? 37   TYR A CD2   1 
ATOM   228  C CE1   . TYR A 1 37  ? -19.795 -22.908 22.495  1.00 13.56 ? 37   TYR A CE1   1 
ATOM   229  C CE2   . TYR A 1 37  ? -20.011 -20.918 23.796  1.00 12.98 ? 37   TYR A CE2   1 
ATOM   230  C CZ    . TYR A 1 37  ? -19.279 -21.705 22.940  1.00 14.04 ? 37   TYR A CZ    1 
ATOM   231  O OH    . TYR A 1 37  ? -18.035 -21.309 22.542  1.00 14.82 ? 37   TYR A OH    1 
ATOM   232  N N     . ASN A 1 38  ? -23.307 -21.993 27.118  1.00 11.37 ? 38   ASN A N     1 
ATOM   233  C CA    . ASN A 1 38  ? -22.998 -21.226 28.315  1.00 12.07 ? 38   ASN A CA    1 
ATOM   234  C C     . ASN A 1 38  ? -23.355 -22.076 29.529  1.00 12.35 ? 38   ASN A C     1 
ATOM   235  O O     . ASN A 1 38  ? -24.503 -22.501 29.678  1.00 12.03 ? 38   ASN A O     1 
ATOM   236  C CB    . ASN A 1 38  ? -23.745 -19.916 28.313  1.00 12.00 ? 38   ASN A CB    1 
ATOM   237  C CG    . ASN A 1 38  ? -23.421 -19.118 29.551  1.00 13.69 ? 38   ASN A CG    1 
ATOM   238  O OD1   . ASN A 1 38  ? -23.979 -19.360 30.625  1.00 15.15 ? 38   ASN A OD1   1 
ATOM   239  N ND2   . ASN A 1 38  ? -22.480 -18.206 29.419  1.00 13.87 ? 38   ASN A ND2   1 
ATOM   240  N N     . PHE A 1 39  ? -22.387 -22.292 30.419  1.00 11.72 ? 39   PHE A N     1 
ATOM   241  C CA    . PHE A 1 39  ? -22.597 -23.217 31.526  1.00 12.00 ? 39   PHE A CA    1 
ATOM   242  C C     . PHE A 1 39  ? -23.279 -22.547 32.718  1.00 12.39 ? 39   PHE A C     1 
ATOM   243  O O     . PHE A 1 39  ? -23.640 -23.247 33.661  1.00 13.17 ? 39   PHE A O     1 
ATOM   244  C CB    . PHE A 1 39  ? -21.275 -23.825 31.993  1.00 12.48 ? 39   PHE A CB    1 
ATOM   245  C CG    . PHE A 1 39  ? -20.652 -24.844 31.048  1.00 12.57 ? 39   PHE A CG    1 
ATOM   246  C CD1   . PHE A 1 39  ? -21.339 -25.371 29.957  1.00 14.05 ? 39   PHE A CD1   1 
ATOM   247  C CD2   . PHE A 1 39  ? -19.404 -25.360 31.314  1.00 14.26 ? 39   PHE A CD2   1 
ATOM   248  C CE1   . PHE A 1 39  ? -20.753 -26.335 29.140  1.00 15.13 ? 39   PHE A CE1   1 
ATOM   249  C CE2   . PHE A 1 39  ? -18.836 -26.339 30.501  1.00 15.56 ? 39   PHE A CE2   1 
ATOM   250  C CZ    . PHE A 1 39  ? -19.502 -26.815 29.421  1.00 15.49 ? 39   PHE A CZ    1 
ATOM   251  N N     . ASP A 1 40  ? -23.459 -21.235 32.682  1.00 11.90 ? 40   ASP A N     1 
ATOM   252  C CA    . ASP A 1 40  ? -24.134 -20.518 33.752  1.00 13.82 ? 40   ASP A CA    1 
ATOM   253  C C     . ASP A 1 40  ? -25.646 -20.505 33.554  1.00 13.03 ? 40   ASP A C     1 
ATOM   254  O O     . ASP A 1 40  ? -26.383 -20.706 34.527  1.00 14.71 ? 40   ASP A O     1 
ATOM   255  C CB    . ASP A 1 40  ? -23.563 -19.130 33.925  1.00 13.47 ? 40   ASP A CB    1 
ATOM   256  C CG    . ASP A 1 40  ? -22.064 -19.220 34.125  1.00 16.97 ? 40   ASP A CG    1 
ATOM   257  O OD1   . ASP A 1 40  ? -21.677 -19.734 35.200  1.00 17.53 ? 40   ASP A OD1   1 
ATOM   258  O OD2   . ASP A 1 40  ? -21.337 -18.855 33.158  1.00 17.32 ? 40   ASP A OD2   1 
ATOM   259  N N     . LEU A 1 41  ? -26.077 -20.316 32.297  1.00 13.17 ? 41   LEU A N     1 
ATOM   260  C CA    . LEU A 1 41  ? -27.485 -20.132 31.978  1.00 12.84 ? 41   LEU A CA    1 
ATOM   261  C C     . LEU A 1 41  ? -28.087 -21.476 31.575  1.00 13.29 ? 41   LEU A C     1 
ATOM   262  O O     . LEU A 1 41  ? -28.589 -21.645 30.475  1.00 12.83 ? 41   LEU A O     1 
ATOM   263  C CB    . LEU A 1 41  ? -27.638 -19.066 30.884  1.00 13.45 ? 41   LEU A CB    1 
ATOM   264  C CG    . LEU A 1 41  ? -27.257 -17.643 31.290  1.00 14.84 ? 41   LEU A CG    1 
ATOM   265  C CD1   . LEU A 1 41  ? -27.181 -16.746 30.049  1.00 14.68 ? 41   LEU A CD1   1 
ATOM   266  C CD2   . LEU A 1 41  ? -28.181 -17.049 32.329  1.00 16.48 ? 41   LEU A CD2   1 
ATOM   267  N N     . LEU A 1 42  ? -28.090 -22.420 32.523  1.00 12.50 ? 42   LEU A N     1 
ATOM   268  C CA    . LEU A 1 42  ? -28.613 -23.751 32.285  1.00 13.52 ? 42   LEU A CA    1 
ATOM   269  C C     . LEU A 1 42  ? -30.121 -23.667 32.138  1.00 13.74 ? 42   LEU A C     1 
ATOM   270  O O     . LEU A 1 42  ? -30.746 -22.824 32.754  1.00 17.03 ? 42   LEU A O     1 
ATOM   271  C CB    . LEU A 1 42  ? -28.216 -24.710 33.383  1.00 12.79 ? 42   LEU A CB    1 
ATOM   272  C CG    . LEU A 1 42  ? -26.707 -24.878 33.576  1.00 12.26 ? 42   LEU A CG    1 
ATOM   273  C CD1   . LEU A 1 42  ? -26.457 -25.995 34.565  1.00 12.25 ? 42   LEU A CD1   1 
ATOM   274  C CD2   . LEU A 1 42  ? -25.935 -25.197 32.287  1.00 12.79 ? 42   LEU A CD2   1 
ATOM   275  N N     . THR A 1 43  ? -30.693 -24.529 31.315  1.00 12.57 ? 43   THR A N     1 
ATOM   276  C CA    . THR A 1 43  ? -32.102 -24.448 30.985  1.00 12.73 ? 43   THR A CA    1 
ATOM   277  C C     . THR A 1 43  ? -32.711 -25.837 31.095  1.00 12.72 ? 43   THR A C     1 
ATOM   278  O O     . THR A 1 43  ? -32.007 -26.857 31.033  1.00 13.46 ? 43   THR A O     1 
ATOM   279  C CB    . THR A 1 43  ? -32.306 -23.897 29.562  1.00 14.52 ? 43   THR A CB    1 
ATOM   280  O OG1   . THR A 1 43  ? -31.687 -24.744 28.582  1.00 14.90 ? 43   THR A OG1   1 
ATOM   281  C CG2   . THR A 1 43  ? -31.786 -22.489 29.433  1.00 14.96 ? 43   THR A CG2   1 
ATOM   282  N N     . THR A 1 44  ? -34.051 -25.851 31.115  1.00 12.49 ? 44   THR A N     1 
ATOM   283  C CA    . THR A 1 44  ? -34.823 -27.089 31.095  1.00 11.88 ? 44   THR A CA    1 
ATOM   284  C C     . THR A 1 44  ? -35.926 -26.907 30.061  1.00 12.01 ? 44   THR A C     1 
ATOM   285  O O     . THR A 1 44  ? -37.062 -26.509 30.362  1.00 12.46 ? 44   THR A O     1 
ATOM   286  C CB    . THR A 1 44  ? -35.410 -27.467 32.460  1.00 11.47 ? 44   THR A CB    1 
ATOM   287  O OG1   . THR A 1 44  ? -34.334 -27.620 33.377  1.00 12.32 ? 44   THR A OG1   1 
ATOM   288  C CG2   . THR A 1 44  ? -36.116 -28.806 32.423  1.00 11.89 ? 44   THR A CG2   1 
ATOM   289  N N     . PRO A 1 45  ? -35.630 -27.175 28.789  1.00 12.11 ? 45   PRO A N     1 
ATOM   290  C CA    . PRO A 1 45  ? -36.698 -27.226 27.778  1.00 12.30 ? 45   PRO A CA    1 
ATOM   291  C C     . PRO A 1 45  ? -37.811 -28.172 28.222  1.00 12.45 ? 45   PRO A C     1 
ATOM   292  O O     . PRO A 1 45  ? -37.532 -29.138 28.950  1.00 13.20 ? 45   PRO A O     1 
ATOM   293  C CB    . PRO A 1 45  ? -36.016 -27.694 26.478  1.00 12.03 ? 45   PRO A CB    1 
ATOM   294  C CG    . PRO A 1 45  ? -34.553 -27.864 26.812  1.00 12.83 ? 45   PRO A CG    1 
ATOM   295  C CD    . PRO A 1 45  ? -34.303 -27.520 28.268  1.00 12.30 ? 45   PRO A CD    1 
ATOM   296  N N     . SER A 1 46  ? -39.052 -27.909 27.770  1.00 11.68 ? 46   SER A N     1 
ATOM   297  C CA    . SER A 1 46  ? -40.149 -28.831 28.046  1.00 13.49 ? 46   SER A CA    1 
ATOM   298  C C     . SER A 1 46  ? -39.932 -30.174 27.346  1.00 12.86 ? 46   SER A C     1 
ATOM   299  O O     . SER A 1 46  ? -40.447 -31.191 27.793  1.00 12.96 ? 46   SER A O     1 
ATOM   300  C CB    . SER A 1 46  ? -41.507 -28.239 27.752  1.00 15.78 ? 46   SER A CB    1 
ATOM   301  O OG    . SER A 1 46  ? -41.495 -27.555 26.512  1.00 19.08 ? 46   SER A OG    1 
ATOM   302  N N     . ALA A 1 47  ? -39.209 -30.157 26.219  1.00 11.52 ? 47   ALA A N     1 
ATOM   303  C CA    . ALA A 1 47  ? -38.806 -31.368 25.522  1.00 11.62 ? 47   ALA A CA    1 
ATOM   304  C C     . ALA A 1 47  ? -37.758 -31.012 24.480  1.00 11.50 ? 47   ALA A C     1 
ATOM   305  O O     . ALA A 1 47  ? -37.649 -29.840 24.096  1.00 10.97 ? 47   ALA A O     1 
ATOM   306  C CB    . ALA A 1 47  ? -39.994 -32.025 24.818  1.00 12.37 ? 47   ALA A CB    1 
ATOM   307  N N     . ILE A 1 48  ? -37.029 -32.039 24.033  1.00 11.72 ? 48   ILE A N     1 
ATOM   308  C CA    . ILE A 1 48  ? -36.117 -31.942 22.896  1.00 11.77 ? 48   ILE A CA    1 
ATOM   309  C C     . ILE A 1 48  ? -36.600 -32.949 21.857  1.00 11.82 ? 48   ILE A C     1 
ATOM   310  O O     . ILE A 1 48  ? -36.968 -34.066 22.213  1.00 12.15 ? 48   ILE A O     1 
ATOM   311  C CB    . ILE A 1 48  ? -34.651 -32.239 23.241  1.00 12.07 ? 48   ILE A CB    1 
ATOM   312  C CG1   . ILE A 1 48  ? -34.193 -31.551 24.507  1.00 12.72 ? 48   ILE A CG1   1 
ATOM   313  C CG2   . ILE A 1 48  ? -33.757 -31.826 22.060  1.00 11.88 ? 48   ILE A CG2   1 
ATOM   314  C CD1   . ILE A 1 48  ? -32.905 -32.118 25.077  1.00 13.11 ? 48   ILE A CD1   1 
ATOM   315  N N     . VAL A 1 49  ? -36.614 -32.561 20.587  1.00 11.85 ? 49   VAL A N     1 
ATOM   316  C CA    . VAL A 1 49  ? -36.977 -33.487 19.517  1.00 11.31 ? 49   VAL A CA    1 
ATOM   317  C C     . VAL A 1 49  ? -35.910 -33.389 18.430  1.00 10.84 ? 49   VAL A C     1 
ATOM   318  O O     . VAL A 1 49  ? -35.392 -32.281 18.188  1.00 11.87 ? 49   VAL A O     1 
ATOM   319  C CB    . VAL A 1 49  ? -38.385 -33.103 19.002  1.00 13.19 ? 49   VAL A CB    1 
ATOM   320  C CG1   . VAL A 1 49  ? -38.486 -31.682 18.453  1.00 11.30 ? 49   VAL A CG1   1 
ATOM   321  C CG2   . VAL A 1 49  ? -38.954 -34.093 18.006  1.00 14.35 ? 49   VAL A CG2   1 
ATOM   322  N N     . TRP A 1 50  ? -35.632 -34.529 17.766  1.00 10.85 ? 50   TRP A N     1 
ATOM   323  C CA    . TRP A 1 50  ? -34.655 -34.615 16.691  1.00 11.92 ? 50   TRP A CA    1 
ATOM   324  C C     . TRP A 1 50  ? -35.338 -35.017 15.390  1.00 11.57 ? 50   TRP A C     1 
ATOM   325  O O     . TRP A 1 50  ? -35.298 -36.198 14.991  1.00 12.34 ? 50   TRP A O     1 
ATOM   326  C CB    . TRP A 1 50  ? -33.570 -35.629 17.035  1.00 11.80 ? 50   TRP A CB    1 
ATOM   327  C CG    . TRP A 1 50  ? -32.607 -35.213 18.107  1.00 13.38 ? 50   TRP A CG    1 
ATOM   328  C CD1   . TRP A 1 50  ? -31.335 -34.791 17.860  1.00 14.24 ? 50   TRP A CD1   1 
ATOM   329  C CD2   . TRP A 1 50  ? -32.748 -35.255 19.545  1.00 13.28 ? 50   TRP A CD2   1 
ATOM   330  N NE1   . TRP A 1 50  ? -30.685 -34.512 19.030  1.00 14.62 ? 50   TRP A NE1   1 
ATOM   331  C CE2   . TRP A 1 50  ? -31.516 -34.785 20.075  1.00 13.89 ? 50   TRP A CE2   1 
ATOM   332  C CE3   . TRP A 1 50  ? -33.759 -35.639 20.428  1.00 14.81 ? 50   TRP A CE3   1 
ATOM   333  C CZ2   . TRP A 1 50  ? -31.281 -34.708 21.441  1.00 13.98 ? 50   TRP A CZ2   1 
ATOM   334  C CZ3   . TRP A 1 50  ? -33.515 -35.574 21.787  1.00 14.71 ? 50   TRP A CZ3   1 
ATOM   335  C CH2   . TRP A 1 50  ? -32.291 -35.120 22.279  1.00 14.22 ? 50   TRP A CH2   1 
ATOM   336  N N     . PRO A 1 51  ? -36.015 -34.076 14.715  1.00 11.91 ? 51   PRO A N     1 
ATOM   337  C CA    . PRO A 1 51  ? -36.703 -34.417 13.459  1.00 12.71 ? 51   PRO A CA    1 
ATOM   338  C C     . PRO A 1 51  ? -35.699 -34.906 12.415  1.00 13.25 ? 51   PRO A C     1 
ATOM   339  O O     . PRO A 1 51  ? -34.549 -34.473 12.357  1.00 13.65 ? 51   PRO A O     1 
ATOM   340  C CB    . PRO A 1 51  ? -37.388 -33.134 13.044  1.00 12.09 ? 51   PRO A CB    1 
ATOM   341  C CG    . PRO A 1 51  ? -36.622 -32.049 13.787  1.00 13.13 ? 51   PRO A CG    1 
ATOM   342  C CD    . PRO A 1 51  ? -36.158 -32.659 15.087  1.00 13.24 ? 51   PRO A CD    1 
ATOM   343  N N     . GLN A 1 52  ? -36.187 -35.790 11.537  1.00 13.50 ? 52   GLN A N     1 
ATOM   344  C CA    . GLN A 1 52  ? -35.401 -36.287 10.414  1.00 15.32 ? 52   GLN A CA    1 
ATOM   345  C C     . GLN A 1 52  ? -35.441 -35.362 9.199   1.00 15.14 ? 52   GLN A C     1 
ATOM   346  O O     . GLN A 1 52  ? -34.583 -35.483 8.322   1.00 16.91 ? 52   GLN A O     1 
ATOM   347  C CB    . GLN A 1 52  ? -35.991 -37.622 9.949   1.00 18.43 ? 52   GLN A CB    1 
ATOM   348  C CG    . GLN A 1 52  ? -35.700 -38.815 10.844  1.00 23.31 ? 52   GLN A CG    1 
ATOM   349  C CD    . GLN A 1 52  ? -34.309 -39.355 10.648  1.00 30.55 ? 52   GLN A CD    1 
ATOM   350  O OE1   . GLN A 1 52  ? -33.900 -39.632 9.513   1.00 32.67 ? 52   GLN A OE1   1 
ATOM   351  N NE2   . GLN A 1 52  ? -33.591 -39.547 11.745  1.00 30.36 ? 52   GLN A NE2   1 
ATOM   352  N N     . ASP A 1 53  ? -36.500 -34.565 9.050   1.00 14.66 ? 53   ASP A N     1 
ATOM   353  C CA    . ASP A 1 53  ? -36.741 -33.806 7.829   1.00 15.43 ? 53   ASP A CA    1 
ATOM   354  C C     . ASP A 1 53  ? -37.727 -32.671 8.110   1.00 14.93 ? 53   ASP A C     1 
ATOM   355  O O     . ASP A 1 53  ? -38.220 -32.532 9.244   1.00 15.34 ? 53   ASP A O     1 
ATOM   356  C CB    . ASP A 1 53  ? -37.294 -34.713 6.737   1.00 15.27 ? 53   ASP A CB    1 
ATOM   357  C CG    . ASP A 1 53  ? -38.660 -35.333 6.978   1.00 16.54 ? 53   ASP A CG    1 
ATOM   358  O OD1   . ASP A 1 53  ? -39.281 -35.097 8.054   1.00 14.14 ? 53   ASP A OD1   1 
ATOM   359  O OD2   . ASP A 1 53  ? -39.102 -36.101 6.082   1.00 19.12 ? 53   ASP A OD2   1 
ATOM   360  N N     . THR A 1 54  ? -38.055 -31.890 7.065   1.00 13.58 ? 54   THR A N     1 
ATOM   361  C CA    . THR A 1 54  ? -38.920 -30.736 7.198   1.00 12.80 ? 54   THR A CA    1 
ATOM   362  C C     . THR A 1 54  ? -40.285 -31.146 7.752   1.00 11.59 ? 54   THR A C     1 
ATOM   363  O O     . THR A 1 54  ? -40.851 -30.456 8.579   1.00 13.01 ? 54   THR A O     1 
ATOM   364  C CB    . THR A 1 54  ? -39.065 -30.027 5.850   1.00 12.72 ? 54   THR A CB    1 
ATOM   365  O OG1   . THR A 1 54  ? -37.731 -29.835 5.365   1.00 13.42 ? 54   THR A OG1   1 
ATOM   366  C CG2   . THR A 1 54  ? -39.863 -28.753 5.991   1.00 12.15 ? 54   THR A CG2   1 
ATOM   367  N N     . GLN A 1 55  ? -40.899 -32.211 7.212   1.00 11.89 ? 55   GLN A N     1 
ATOM   368  C CA    . GLN A 1 55  ? -42.200 -32.665 7.675   1.00 11.69 ? 55   GLN A CA    1 
ATOM   369  C C     . GLN A 1 55  ? -42.217 -32.891 9.191   1.00 12.41 ? 55   GLN A C     1 
ATOM   370  O O     . GLN A 1 55  ? -43.143 -32.487 9.891   1.00 12.17 ? 55   GLN A O     1 
ATOM   371  C CB    . GLN A 1 55  ? -42.664 -33.904 6.915   1.00 12.62 ? 55   GLN A CB    1 
ATOM   372  C CG    . GLN A 1 55  ? -44.001 -34.436 7.410   1.00 12.81 ? 55   GLN A CG    1 
ATOM   373  C CD    . GLN A 1 55  ? -43.873 -35.402 8.577   1.00 13.40 ? 55   GLN A CD    1 
ATOM   374  O OE1   . GLN A 1 55  ? -42.966 -36.233 8.621   1.00 13.99 ? 55   GLN A OE1   1 
ATOM   375  N NE2   . GLN A 1 55  ? -44.831 -35.334 9.480   1.00 12.75 ? 55   GLN A NE2   1 
ATOM   376  N N     . GLN A 1 56  ? -41.154 -33.475 9.726   1.00 12.72 ? 56   GLN A N     1 
ATOM   377  C CA    . GLN A 1 56  ? -41.127 -33.792 11.151  1.00 12.69 ? 56   GLN A CA    1 
ATOM   378  C C     . GLN A 1 56  ? -40.925 -32.516 11.975  1.00 11.78 ? 56   GLN A C     1 
ATOM   379  O O     . GLN A 1 56  ? -41.456 -32.418 13.084  1.00 11.32 ? 56   GLN A O     1 
ATOM   380  C CB    . GLN A 1 56  ? -40.096 -34.869 11.420  1.00 13.09 ? 56   GLN A CB    1 
ATOM   381  C CG    . GLN A 1 56  ? -40.514 -36.246 10.893  1.00 13.85 ? 56   GLN A CG    1 
ATOM   382  C CD    . GLN A 1 56  ? -39.608 -37.355 11.361  1.00 14.15 ? 56   GLN A CD    1 
ATOM   383  O OE1   . GLN A 1 56  ? -38.596 -37.127 12.032  1.00 13.32 ? 56   GLN A OE1   1 
ATOM   384  N NE2   . GLN A 1 56  ? -39.984 -38.588 11.018  1.00 15.33 ? 56   GLN A NE2   1 
ATOM   385  N N     . VAL A 1 57  ? -40.225 -31.535 11.399  1.00 12.63 ? 57   VAL A N     1 
ATOM   386  C CA    . VAL A 1 57  ? -40.136 -30.224 12.024  1.00 12.14 ? 57   VAL A CA    1 
ATOM   387  C C     . VAL A 1 57  ? -41.558 -29.665 12.125  1.00 13.07 ? 57   VAL A C     1 
ATOM   388  O O     . VAL A 1 57  ? -41.944 -29.186 13.180  1.00 12.21 ? 57   VAL A O     1 
ATOM   389  C CB    . VAL A 1 57  ? -39.197 -29.254 11.271  1.00 12.77 ? 57   VAL A CB    1 
ATOM   390  C CG1   . VAL A 1 57  ? -39.228 -27.813 11.843  1.00 12.79 ? 57   VAL A CG1   1 
ATOM   391  C CG2   . VAL A 1 57  ? -37.762 -29.791 11.210  1.00 13.60 ? 57   VAL A CG2   1 
ATOM   392  N N     . ALA A 1 58  ? -42.317 -29.686 11.009  1.00 13.04 ? 58   ALA A N     1 
ATOM   393  C CA    . ALA A 1 58  ? -43.653 -29.108 10.983  1.00 13.36 ? 58   ALA A CA    1 
ATOM   394  C C     . ALA A 1 58  ? -44.545 -29.838 11.977  1.00 11.90 ? 58   ALA A C     1 
ATOM   395  O O     . ALA A 1 58  ? -45.306 -29.205 12.714  1.00 12.45 ? 58   ALA A O     1 
ATOM   396  C CB    . ALA A 1 58  ? -44.198 -29.117 9.567   1.00 13.64 ? 58   ALA A CB    1 
ATOM   397  N N     . ALA A 1 59  ? -44.427 -31.166 12.053  1.00 12.26 ? 59   ALA A N     1 
ATOM   398  C CA    . ALA A 1 59  ? -45.221 -31.943 12.992  1.00 12.42 ? 59   ALA A CA    1 
ATOM   399  C C     . ALA A 1 59  ? -44.900 -31.574 14.437  1.00 12.81 ? 59   ALA A C     1 
ATOM   400  O O     . ALA A 1 59  ? -45.812 -31.394 15.268  1.00 13.84 ? 59   ALA A O     1 
ATOM   401  C CB    . ALA A 1 59  ? -45.007 -33.401 12.744  1.00 12.01 ? 59   ALA A CB    1 
ATOM   402  N N     . ALA A 1 60  ? -43.618 -31.401 14.732  1.00 11.41 ? 60   ALA A N     1 
ATOM   403  C CA    . ALA A 1 60  ? -43.224 -31.098 16.107  1.00 13.00 ? 60   ALA A CA    1 
ATOM   404  C C     . ALA A 1 60  ? -43.675 -29.705 16.539  1.00 12.37 ? 60   ALA A C     1 
ATOM   405  O O     . ALA A 1 60  ? -44.135 -29.538 17.667  1.00 12.35 ? 60   ALA A O     1 
ATOM   406  C CB    . ALA A 1 60  ? -41.743 -31.234 16.263  1.00 13.52 ? 60   ALA A CB    1 
ATOM   407  N N     . VAL A 1 61  ? -43.624 -28.741 15.624  1.00 12.00 ? 61   VAL A N     1 
ATOM   408  C CA    . VAL A 1 61  ? -44.109 -27.399 15.910  1.00 11.79 ? 61   VAL A CA    1 
ATOM   409  C C     . VAL A 1 61  ? -45.590 -27.448 16.275  1.00 12.63 ? 61   VAL A C     1 
ATOM   410  O O     . VAL A 1 61  ? -46.046 -26.800 17.216  1.00 13.63 ? 61   VAL A O     1 
ATOM   411  C CB    . VAL A 1 61  ? -43.837 -26.451 14.752  1.00 12.24 ? 61   VAL A CB    1 
ATOM   412  C CG1   . VAL A 1 61  ? -44.590 -25.143 14.878  1.00 13.29 ? 61   VAL A CG1   1 
ATOM   413  C CG2   . VAL A 1 61  ? -42.351 -26.205 14.586  1.00 12.19 ? 61   VAL A CG2   1 
ATOM   414  N N     . LYS A 1 62  ? -46.355 -28.186 15.495  1.00 13.18 ? 62   LYS A N     1 
ATOM   415  C CA    . LYS A 1 62  ? -47.772 -28.339 15.782  1.00 14.01 ? 62   LYS A CA    1 
ATOM   416  C C     . LYS A 1 62  ? -48.013 -28.935 17.168  1.00 13.52 ? 62   LYS A C     1 
ATOM   417  O O     . LYS A 1 62  ? -48.920 -28.499 17.868  1.00 14.84 ? 62   LYS A O     1 
ATOM   418  C CB    . LYS A 1 62  ? -48.468 -29.207 14.731  1.00 16.56 ? 62   LYS A CB    1 
ATOM   419  C CG    . LYS A 1 62  ? -50.002 -29.179 14.906  1.00 20.21 ? 62   LYS A CG    1 
ATOM   420  C CD    . LYS A 1 62  ? -50.786 -29.809 13.765  1.00 23.80 ? 62   LYS A CD    1 
ATOM   421  C CE    . LYS A 1 62  ? -52.258 -29.598 14.011  1.00 27.14 ? 62   LYS A CE    1 
ATOM   422  N NZ    . LYS A 1 62  ? -52.647 -30.486 15.105  1.00 31.35 ? 62   LYS A NZ    1 
ATOM   423  N N     . CYS A 1 63  ? -47.212 -29.929 17.567  1.00 13.70 ? 63   CYS A N     1 
ATOM   424  C CA    . CYS A 1 63  ? -47.354 -30.513 18.884  1.00 13.41 ? 63   CYS A CA    1 
ATOM   425  C C     . CYS A 1 63  ? -47.220 -29.438 19.958  1.00 13.50 ? 63   CYS A C     1 
ATOM   426  O O     . CYS A 1 63  ? -48.019 -29.403 20.892  1.00 13.26 ? 63   CYS A O     1 
ATOM   427  C CB    . CYS A 1 63  ? -46.314 -31.562 19.203  1.00 14.14 ? 63   CYS A CB    1 
ATOM   428  S SG    . CYS A 1 63  ? -46.398 -33.017 18.144  1.00 18.05 ? 63   CYS A SG    1 
ATOM   429  N N     . ALA A 1 64  ? -46.208 -28.570 19.829  1.00 13.96 ? 64   ALA A N     1 
ATOM   430  C CA    . ALA A 1 64  ? -46.044 -27.455 20.754  1.00 14.01 ? 64   ALA A CA    1 
ATOM   431  C C     . ALA A 1 64  ? -47.252 -26.524 20.720  1.00 17.33 ? 64   ALA A C     1 
ATOM   432  O O     . ALA A 1 64  ? -47.838 -26.211 21.775  1.00 15.00 ? 64   ALA A O     1 
ATOM   433  C CB    . ALA A 1 64  ? -44.744 -26.704 20.510  1.00 15.57 ? 64   ALA A CB    1 
ATOM   434  N N     . VAL A 1 65  ? -47.666 -26.115 19.515  1.00 15.63 ? 65   VAL A N     1 
ATOM   435  C CA    . VAL A 1 65  ? -48.775 -25.181 19.397  1.00 16.66 ? 65   VAL A CA    1 
ATOM   436  C C     . VAL A 1 65  ? -50.019 -25.769 20.061  1.00 14.85 ? 65   VAL A C     1 
ATOM   437  O O     . VAL A 1 65  ? -50.699 -25.038 20.769  1.00 16.66 ? 65   VAL A O     1 
ATOM   438  C CB    . VAL A 1 65  ? -49.047 -24.736 17.948  1.00 17.58 ? 65   VAL A CB    1 
ATOM   439  C CG1   . VAL A 1 65  ? -50.375 -24.002 17.780  1.00 18.78 ? 65   VAL A CG1   1 
ATOM   440  C CG2   . VAL A 1 65  ? -47.866 -23.890 17.464  1.00 17.78 ? 65   VAL A CG2   1 
ATOM   441  N N     . ASP A 1 66  ? -50.287 -27.060 19.838  1.00 15.08 ? 66   ASP A N     1 
ATOM   442  C CA    . ASP A 1 66  ? -51.474 -27.732 20.365  1.00 17.69 ? 66   ASP A CA    1 
ATOM   443  C C     . ASP A 1 66  ? -51.477 -27.754 21.887  1.00 17.73 ? 66   ASP A C     1 
ATOM   444  O O     . ASP A 1 66  ? -52.562 -27.889 22.466  1.00 18.54 ? 66   ASP A O     1 
ATOM   445  C CB    . ASP A 1 66  ? -51.622 -29.154 19.839  1.00 18.33 ? 66   ASP A CB    1 
ATOM   446  C CG    . ASP A 1 66  ? -52.001 -29.349 18.366  1.00 22.16 ? 66   ASP A CG    1 
ATOM   447  O OD1   . ASP A 1 66  ? -52.404 -28.367 17.731  1.00 23.64 ? 66   ASP A OD1   1 
ATOM   448  O OD2   . ASP A 1 66  ? -51.870 -30.508 17.886  1.00 27.87 ? 66   ASP A OD2   1 
ATOM   449  N N     . SER A 1 67  ? -50.300 -27.668 22.534  1.00 16.76 ? 67   SER A N     1 
ATOM   450  C CA    . SER A 1 67  ? -50.201 -27.694 23.984  1.00 17.54 ? 67   SER A CA    1 
ATOM   451  C C     . SER A 1 67  ? -49.820 -26.343 24.580  1.00 17.52 ? 67   SER A C     1 
ATOM   452  O O     . SER A 1 67  ? -49.439 -26.288 25.755  1.00 17.76 ? 67   SER A O     1 
ATOM   453  C CB    . SER A 1 67  ? -49.243 -28.736 24.449  1.00 19.76 ? 67   SER A CB    1 
ATOM   454  O OG    . SER A 1 67  ? -49.805 -30.026 24.308  1.00 22.71 ? 67   SER A OG    1 
ATOM   455  N N     . ASP A 1 68  ? -49.911 -25.274 23.794  1.00 17.13 ? 68   ASP A N     1 
ATOM   456  C CA    . ASP A 1 68  ? -49.603 -23.919 24.228  1.00 18.92 ? 68   ASP A CA    1 
ATOM   457  C C     . ASP A 1 68  ? -48.168 -23.828 24.750  1.00 16.91 ? 68   ASP A C     1 
ATOM   458  O O     . ASP A 1 68  ? -47.880 -23.197 25.780  1.00 18.65 ? 68   ASP A O     1 
ATOM   459  C CB    . ASP A 1 68  ? -50.517 -23.436 25.343  1.00 21.74 ? 68   ASP A CB    1 
ATOM   460  C CG    . ASP A 1 68  ? -50.495 -21.933 25.596  1.00 27.65 ? 68   ASP A CG    1 
ATOM   461  O OD1   . ASP A 1 68  ? -50.061 -21.177 24.689  1.00 37.52 ? 68   ASP A OD1   1 
ATOM   462  O OD2   . ASP A 1 68  ? -50.890 -21.508 26.720  1.00 40.34 ? 68   ASP A OD2   1 
ATOM   463  N N     . ILE A 1 69  ? -47.274 -24.466 24.010  1.00 14.94 ? 69   ILE A N     1 
ATOM   464  C CA    . ILE A 1 69  ? -45.848 -24.399 24.283  1.00 13.97 ? 69   ILE A CA    1 
ATOM   465  C C     . ILE A 1 69  ? -45.177 -23.664 23.121  1.00 13.53 ? 69   ILE A C     1 
ATOM   466  O O     . ILE A 1 69  ? -45.508 -23.891 21.946  1.00 13.40 ? 69   ILE A O     1 
ATOM   467  C CB    . ILE A 1 69  ? -45.342 -25.833 24.481  1.00 15.36 ? 69   ILE A CB    1 
ATOM   468  C CG1   . ILE A 1 69  ? -45.931 -26.426 25.778  1.00 17.23 ? 69   ILE A CG1   1 
ATOM   469  C CG2   . ILE A 1 69  ? -43.817 -25.929 24.477  1.00 15.38 ? 69   ILE A CG2   1 
ATOM   470  C CD1   . ILE A 1 69  ? -45.676 -27.904 25.903  1.00 19.59 ? 69   ILE A CD1   1 
ATOM   471  N N     . LYS A 1 70  ? -44.190 -22.839 23.463  1.00 12.53 ? 70   LYS A N     1 
ATOM   472  C CA    . LYS A 1 70  ? -43.430 -22.085 22.471  1.00 12.93 ? 70   LYS A CA    1 
ATOM   473  C C     . LYS A 1 70  ? -42.200 -22.883 22.041  1.00 12.33 ? 70   LYS A C     1 
ATOM   474  O O     . LYS A 1 70  ? -41.927 -23.952 22.576  1.00 12.22 ? 70   LYS A O     1 
ATOM   475  C CB    . LYS A 1 70  ? -43.131 -20.701 23.012  1.00 14.11 ? 70   LYS A CB    1 
ATOM   476  C CG    . LYS A 1 70  ? -44.363 -19.874 23.196  1.00 15.52 ? 70   LYS A CG    1 
ATOM   477  C CD    . LYS A 1 70  ? -44.156 -18.481 23.732  1.00 16.74 ? 70   LYS A CD    1 
ATOM   478  C CE    . LYS A 1 70  ? -45.436 -17.742 24.014  1.00 20.65 ? 70   LYS A CE    1 
ATOM   479  N NZ    . LYS A 1 70  ? -46.304 -17.535 22.844  1.00 20.95 ? 70   LYS A NZ    1 
ATOM   480  N N     . VAL A 1 71  ? -41.480 -22.388 21.021  1.00 11.86 ? 71   VAL A N     1 
ATOM   481  C CA    . VAL A 1 71  ? -40.534 -23.208 20.264  1.00 12.60 ? 71   VAL A CA    1 
ATOM   482  C C     . VAL A 1 71  ? -39.290 -22.400 19.922  1.00 12.40 ? 71   VAL A C     1 
ATOM   483  O O     . VAL A 1 71  ? -39.368 -21.224 19.515  1.00 11.62 ? 71   VAL A O     1 
ATOM   484  C CB    . VAL A 1 71  ? -41.152 -23.707 18.938  1.00 12.53 ? 71   VAL A CB    1 
ATOM   485  C CG1   . VAL A 1 71  ? -40.113 -24.460 18.106  1.00 11.64 ? 71   VAL A CG1   1 
ATOM   486  C CG2   . VAL A 1 71  ? -42.448 -24.495 19.148  1.00 13.29 ? 71   VAL A CG2   1 
ATOM   487  N N     . GLN A 1 72  ? -38.126 -23.047 20.072  1.00 11.02 ? 72   GLN A N     1 
ATOM   488  C CA    . GLN A 1 72  ? -36.919 -22.589 19.407  1.00 10.62 ? 72   GLN A CA    1 
ATOM   489  C C     . GLN A 1 72  ? -36.257 -23.782 18.758  1.00 10.30 ? 72   GLN A C     1 
ATOM   490  O O     . GLN A 1 72  ? -36.178 -24.873 19.345  1.00 11.54 ? 72   GLN A O     1 
ATOM   491  C CB    . GLN A 1 72  ? -35.868 -21.906 20.270  1.00 10.61 ? 72   GLN A CB    1 
ATOM   492  C CG    . GLN A 1 72  ? -36.286 -20.545 20.778  1.00 10.99 ? 72   GLN A CG    1 
ATOM   493  C CD    . GLN A 1 72  ? -36.093 -19.469 19.746  1.00 11.21 ? 72   GLN A CD    1 
ATOM   494  O OE1   . GLN A 1 72  ? -35.031 -18.845 19.679  1.00 11.97 ? 72   GLN A OE1   1 
ATOM   495  N NE2   . GLN A 1 72  ? -37.085 -19.284 18.878  1.00 11.33 ? 72   GLN A NE2   1 
ATOM   496  N N     . PRO A 1 73  ? -35.675 -23.577 17.552  1.00 11.16 ? 73   PRO A N     1 
ATOM   497  C CA    . PRO A 1 73  ? -34.768 -24.568 16.990  1.00 10.56 ? 73   PRO A CA    1 
ATOM   498  C C     . PRO A 1 73  ? -33.360 -24.459 17.569  1.00 10.82 ? 73   PRO A C     1 
ATOM   499  O O     . PRO A 1 73  ? -32.954 -23.417 18.106  1.00 10.96 ? 73   PRO A O     1 
ATOM   500  C CB    . PRO A 1 73  ? -34.794 -24.206 15.494  1.00 10.71 ? 73   PRO A CB    1 
ATOM   501  C CG    . PRO A 1 73  ? -34.879 -22.709 15.517  1.00 10.63 ? 73   PRO A CG    1 
ATOM   502  C CD    . PRO A 1 73  ? -35.827 -22.406 16.665  1.00 10.24 ? 73   PRO A CD    1 
ATOM   503  N N     . LYS A 1 74  ? -32.607 -25.532 17.396  1.00 10.37 ? 74   LYS A N     1 
ATOM   504  C CA    . LYS A 1 74  ? -31.198 -25.536 17.743  1.00 11.57 ? 74   LYS A CA    1 
ATOM   505  C C     . LYS A 1 74  ? -30.428 -26.261 16.642  1.00 11.32 ? 74   LYS A C     1 
ATOM   506  O O     . LYS A 1 74  ? -30.707 -27.415 16.317  1.00 10.92 ? 74   LYS A O     1 
ATOM   507  C CB    . LYS A 1 74  ? -30.967 -26.209 19.103  1.00 13.53 ? 74   LYS A CB    1 
ATOM   508  C CG    . LYS A 1 74  ? -29.539 -26.064 19.617  1.00 17.05 ? 74   LYS A CG    1 
ATOM   509  C CD    . LYS A 1 74  ? -29.395 -26.291 21.116  1.00 20.13 ? 74   LYS A CD    1 
ATOM   510  C CE    . LYS A 1 74  ? -29.531 -27.698 21.517  1.00 23.29 ? 74   LYS A CE    1 
ATOM   511  N NZ    . LYS A 1 74  ? -28.295 -28.473 21.317  1.00 23.28 ? 74   LYS A NZ    1 
ATOM   512  N N     . SER A 1 75  ? -29.432 -25.570 16.089  1.00 10.40 ? 75   SER A N     1 
ATOM   513  C CA    . SER A 1 75  ? -28.611 -26.126 15.021  1.00 10.20 ? 75   SER A CA    1 
ATOM   514  C C     . SER A 1 75  ? -27.230 -26.482 15.579  1.00 11.10 ? 75   SER A C     1 
ATOM   515  O O     . SER A 1 75  ? -27.002 -27.620 15.968  1.00 13.51 ? 75   SER A O     1 
ATOM   516  C CB    . SER A 1 75  ? -28.580 -25.190 13.846  1.00 11.83 ? 75   SER A CB    1 
ATOM   517  O OG    . SER A 1 75  ? -29.834 -25.086 13.183  1.00 10.74 ? 75   SER A OG    1 
ATOM   518  N N     . GLY A 1 76  ? -26.345 -25.502 15.795  1.00 10.95 ? 76   GLY A N     1 
ATOM   519  C CA    . GLY A 1 76  ? -25.047 -25.778 16.396  1.00 11.96 ? 76   GLY A CA    1 
ATOM   520  C C     . GLY A 1 76  ? -24.979 -25.518 17.900  1.00 12.38 ? 76   GLY A C     1 
ATOM   521  O O     . GLY A 1 76  ? -23.995 -25.926 18.566  1.00 11.81 ? 76   GLY A O     1 
ATOM   522  N N     . GLY A 1 77  ? -25.999 -24.840 18.444  1.00 11.09 ? 77   GLY A N     1 
ATOM   523  C CA    . GLY A 1 77  ? -26.063 -24.608 19.875  1.00 11.32 ? 77   GLY A CA    1 
ATOM   524  C C     . GLY A 1 77  ? -25.121 -23.526 20.415  1.00 11.68 ? 77   GLY A C     1 
ATOM   525  O O     . GLY A 1 77  ? -24.923 -23.467 21.620  1.00 13.68 ? 77   GLY A O     1 
ATOM   526  N N     . HIS A 1 78  ? -24.535 -22.661 19.557  1.00 10.90 ? 78   HIS A N     1 
ATOM   527  C CA    . HIS A 1 78  ? -23.574 -21.677 20.024  1.00 12.05 ? 78   HIS A CA    1 
ATOM   528  C C     . HIS A 1 78  ? -24.212 -20.427 20.656  1.00 10.85 ? 78   HIS A C     1 
ATOM   529  O O     . HIS A 1 78  ? -23.491 -19.535 21.116  1.00 12.85 ? 78   HIS A O     1 
ATOM   530  C CB    . HIS A 1 78  ? -22.685 -21.244 18.848  1.00 11.46 ? 78   HIS A CB    1 
ATOM   531  C CG    . HIS A 1 78  ? -21.324 -21.896 18.861  1.00 11.63 ? 78   HIS A CG    1 
ATOM   532  N ND1   . HIS A 1 78  ? -20.167 -21.315 19.342  1.00 12.00 ? 78   HIS A ND1   1 
ATOM   533  C CD2   . HIS A 1 78  ? -21.003 -23.129 18.434  1.00 11.52 ? 78   HIS A CD2   1 
ATOM   534  C CE1   . HIS A 1 78  ? -19.189 -22.216 19.220  1.00 12.15 ? 78   HIS A CE1   1 
ATOM   535  N NE2   . HIS A 1 78  ? -19.663 -23.314 18.687  1.00 13.05 ? 78   HIS A NE2   1 
ATOM   536  N N     . ASN A 1 79  ? -25.539 -20.322 20.724  1.00 10.42 ? 79   ASN A N     1 
ATOM   537  C CA    . ASN A 1 79  ? -26.172 -19.152 21.343  1.00 10.29 ? 79   ASN A CA    1 
ATOM   538  C C     . ASN A 1 79  ? -25.663 -18.936 22.781  1.00 10.08 ? 79   ASN A C     1 
ATOM   539  O O     . ASN A 1 79  ? -25.695 -19.854 23.625  1.00 9.76  ? 79   ASN A O     1 
ATOM   540  C CB    . ASN A 1 79  ? -27.675 -19.341 21.412  1.00 10.50 ? 79   ASN A CB    1 
ATOM   541  C CG    . ASN A 1 79  ? -28.407 -18.096 21.861  1.00 11.29 ? 79   ASN A CG    1 
ATOM   542  O OD1   . ASN A 1 79  ? -28.676 -17.937 23.062  1.00 12.26 ? 79   ASN A OD1   1 
ATOM   543  N ND2   . ASN A 1 79  ? -28.760 -17.228 20.923  1.00 10.41 ? 79   ASN A ND2   1 
ATOM   544  N N     . TYR A 1 80  ? -25.298 -17.678 23.097  1.00 9.52  ? 80   TYR A N     1 
ATOM   545  C CA    . TYR A 1 80  ? -24.682 -17.355 24.372  1.00 10.65 ? 80   TYR A CA    1 
ATOM   546  C C     . TYR A 1 80  ? -25.662 -17.300 25.544  1.00 11.64 ? 80   TYR A C     1 
ATOM   547  O O     . TYR A 1 80  ? -25.216 -17.242 26.699  1.00 11.90 ? 80   TYR A O     1 
ATOM   548  C CB    . TYR A 1 80  ? -23.912 -16.035 24.259  1.00 11.85 ? 80   TYR A CB    1 
ATOM   549  C CG    . TYR A 1 80  ? -22.565 -16.135 23.565  1.00 11.93 ? 80   TYR A CG    1 
ATOM   550  C CD1   . TYR A 1 80  ? -22.024 -17.354 23.175  1.00 11.87 ? 80   TYR A CD1   1 
ATOM   551  C CD2   . TYR A 1 80  ? -21.819 -14.987 23.354  1.00 12.99 ? 80   TYR A CD2   1 
ATOM   552  C CE1   . TYR A 1 80  ? -20.742 -17.419 22.642  1.00 13.46 ? 80   TYR A CE1   1 
ATOM   553  C CE2   . TYR A 1 80  ? -20.550 -15.051 22.818  1.00 14.18 ? 80   TYR A CE2   1 
ATOM   554  C CZ    . TYR A 1 80  ? -20.009 -16.266 22.486  1.00 14.76 ? 80   TYR A CZ    1 
ATOM   555  O OH    . TYR A 1 80  ? -18.757 -16.339 21.934  1.00 20.33 ? 80   TYR A OH    1 
ATOM   556  N N     . GLY A 1 81  ? -26.972 -17.334 25.265  1.00 11.40 ? 81   GLY A N     1 
ATOM   557  C CA    . GLY A 1 81  ? -27.965 -17.551 26.300  1.00 11.64 ? 81   GLY A CA    1 
ATOM   558  C C     . GLY A 1 81  ? -28.634 -18.923 26.247  1.00 11.34 ? 81   GLY A C     1 
ATOM   559  O O     . GLY A 1 81  ? -29.640 -19.122 26.919  1.00 11.62 ? 81   GLY A O     1 
ATOM   560  N N     . ASN A 1 82  ? -28.095 -19.863 25.466  1.00 11.30 ? 82   ASN A N     1 
ATOM   561  C CA    . ASN A 1 82  ? -28.712 -21.156 25.258  1.00 10.30 ? 82   ASN A CA    1 
ATOM   562  C C     . ASN A 1 82  ? -30.169 -21.037 24.815  1.00 9.93  ? 82   ASN A C     1 
ATOM   563  O O     . ASN A 1 82  ? -30.998 -21.874 25.134  1.00 11.08 ? 82   ASN A O     1 
ATOM   564  C CB    . ASN A 1 82  ? -28.586 -22.086 26.456  1.00 11.14 ? 82   ASN A CB    1 
ATOM   565  C CG    . ASN A 1 82  ? -27.153 -22.271 26.890  1.00 10.58 ? 82   ASN A CG    1 
ATOM   566  O OD1   . ASN A 1 82  ? -26.251 -22.524 26.077  1.00 11.29 ? 82   ASN A OD1   1 
ATOM   567  N ND2   . ASN A 1 82  ? -26.935 -22.168 28.174  1.00 11.49 ? 82   ASN A ND2   1 
ATOM   568  N N     . TYR A 1 83  ? -30.465 -20.061 23.972  1.00 10.72 ? 83   TYR A N     1 
ATOM   569  C CA    . TYR A 1 83  ? -31.843 -19.780 23.597  1.00 10.38 ? 83   TYR A CA    1 
ATOM   570  C C     . TYR A 1 83  ? -32.458 -20.893 22.744  1.00 11.52 ? 83   TYR A C     1 
ATOM   571  O O     . TYR A 1 83  ? -33.670 -21.044 22.730  1.00 11.94 ? 83   TYR A O     1 
ATOM   572  C CB    . TYR A 1 83  ? -32.009 -18.461 22.830  1.00 10.50 ? 83   TYR A CB    1 
ATOM   573  C CG    . TYR A 1 83  ? -31.756 -17.153 23.566  1.00 10.97 ? 83   TYR A CG    1 
ATOM   574  C CD1   . TYR A 1 83  ? -31.599 -17.107 24.940  1.00 10.66 ? 83   TYR A CD1   1 
ATOM   575  C CD2   . TYR A 1 83  ? -31.644 -15.962 22.859  1.00 10.63 ? 83   TYR A CD2   1 
ATOM   576  C CE1   . TYR A 1 83  ? -31.328 -15.906 25.566  1.00 11.31 ? 83   TYR A CE1   1 
ATOM   577  C CE2   . TYR A 1 83  ? -31.405 -14.756 23.486  1.00 11.28 ? 83   TYR A CE2   1 
ATOM   578  C CZ    . TYR A 1 83  ? -31.190 -14.736 24.843  1.00 11.80 ? 83   TYR A CZ    1 
ATOM   579  O OH    . TYR A 1 83  ? -30.935 -13.556 25.492  1.00 12.90 ? 83   TYR A OH    1 
ATOM   580  N N     . GLY A 1 84  ? -31.647 -21.694 22.055  1.00 10.15 ? 84   GLY A N     1 
ATOM   581  C CA    . GLY A 1 84  ? -32.159 -22.831 21.317  1.00 11.47 ? 84   GLY A CA    1 
ATOM   582  C C     . GLY A 1 84  ? -32.655 -23.959 22.228  1.00 11.82 ? 84   GLY A C     1 
ATOM   583  O O     . GLY A 1 84  ? -33.273 -24.917 21.749  1.00 12.83 ? 84   GLY A O     1 
ATOM   584  N N     . SER A 1 85  ? -32.414 -23.793 23.539  1.00 11.75 ? 85   SER A N     1 
ATOM   585  C CA    . SER A 1 85  ? -32.898 -24.713 24.558  1.00 11.39 ? 85   SER A CA    1 
ATOM   586  C C     . SER A 1 85  ? -33.669 -23.933 25.618  1.00 13.10 ? 85   SER A C     1 
ATOM   587  O O     . SER A 1 85  ? -33.570 -24.238 26.807  1.00 13.43 ? 85   SER A O     1 
ATOM   588  C CB    . SER A 1 85  ? -31.757 -25.441 25.195  1.00 11.43 ? 85   SER A CB    1 
ATOM   589  O OG    . SER A 1 85  ? -30.996 -26.180 24.242  1.00 10.27 ? 85   SER A OG    1 
ATOM   590  N N     . THR A 1 86  ? -34.451 -22.938 25.199  1.00 12.27 ? 86   THR A N     1 
ATOM   591  C CA    . THR A 1 86  ? -35.130 -22.074 26.157  1.00 12.23 ? 86   THR A CA    1 
ATOM   592  C C     . THR A 1 86  ? -35.990 -22.902 27.126  1.00 11.96 ? 86   THR A C     1 
ATOM   593  O O     . THR A 1 86  ? -36.762 -23.764 26.734  1.00 11.82 ? 86   THR A O     1 
ATOM   594  C CB    . THR A 1 86  ? -35.998 -21.045 25.425  1.00 12.36 ? 86   THR A CB    1 
ATOM   595  O OG1   . THR A 1 86  ? -35.161 -20.075 24.769  1.00 13.06 ? 86   THR A OG1   1 
ATOM   596  C CG2   . THR A 1 86  ? -36.931 -20.312 26.375  1.00 11.67 ? 86   THR A CG2   1 
ATOM   597  N N     . THR A 1 87  ? -35.912 -22.534 28.406  1.00 11.13 ? 87   THR A N     1 
ATOM   598  C CA    . THR A 1 87  ? -36.675 -23.213 29.452  1.00 11.46 ? 87   THR A CA    1 
ATOM   599  C C     . THR A 1 87  ? -38.171 -23.160 29.141  1.00 11.03 ? 87   THR A C     1 
ATOM   600  O O     . THR A 1 87  ? -38.714 -22.124 28.785  1.00 11.20 ? 87   THR A O     1 
ATOM   601  C CB    . THR A 1 87  ? -36.329 -22.616 30.810  1.00 12.58 ? 87   THR A CB    1 
ATOM   602  O OG1   . THR A 1 87  ? -34.995 -23.003 31.176  1.00 13.31 ? 87   THR A OG1   1 
ATOM   603  C CG2   . THR A 1 87  ? -37.274 -23.126 31.891  1.00 13.19 ? 87   THR A CG2   1 
ATOM   604  N N     . GLY A 1 88  ? -38.812 -24.321 29.254  1.00 12.25 ? 88   GLY A N     1 
ATOM   605  C CA    . GLY A 1 88  ? -40.245 -24.434 29.156  1.00 13.35 ? 88   GLY A CA    1 
ATOM   606  C C     . GLY A 1 88  ? -40.732 -24.513 27.712  1.00 14.30 ? 88   GLY A C     1 
ATOM   607  O O     . GLY A 1 88  ? -41.908 -24.723 27.481  1.00 16.43 ? 88   GLY A O     1 
ATOM   608  N N     . GLU A 1 89  ? -39.817 -24.361 26.745  1.00 12.59 ? 89   GLU A N     1 
ATOM   609  C CA    . GLU A 1 89  ? -40.168 -24.429 25.349  1.00 12.88 ? 89   GLU A CA    1 
ATOM   610  C C     . GLU A 1 89  ? -39.642 -25.716 24.722  1.00 12.35 ? 89   GLU A C     1 
ATOM   611  O O     . GLU A 1 89  ? -38.780 -26.427 25.252  1.00 11.91 ? 89   GLU A O     1 
ATOM   612  C CB    . GLU A 1 89  ? -39.594 -23.209 24.638  1.00 13.79 ? 89   GLU A CB    1 
ATOM   613  C CG    . GLU A 1 89  ? -40.161 -21.888 25.135  1.00 13.77 ? 89   GLU A CG    1 
ATOM   614  C CD    . GLU A 1 89  ? -39.753 -20.682 24.322  1.00 11.88 ? 89   GLU A CD    1 
ATOM   615  O OE1   . GLU A 1 89  ? -40.168 -19.575 24.757  1.00 12.65 ? 89   GLU A OE1   1 
ATOM   616  O OE2   . GLU A 1 89  ? -38.986 -20.828 23.307  1.00 11.53 ? 89   GLU A OE2   1 
ATOM   617  N N     . LEU A 1 90  ? -40.229 -26.022 23.570  1.00 11.89 ? 90   LEU A N     1 
ATOM   618  C CA    . LEU A 1 90  ? -39.745 -27.129 22.763  1.00 11.71 ? 90   LEU A CA    1 
ATOM   619  C C     . LEU A 1 90  ? -38.438 -26.712 22.103  1.00 11.95 ? 90   LEU A C     1 
ATOM   620  O O     . LEU A 1 90  ? -38.357 -25.664 21.470  1.00 13.84 ? 90   LEU A O     1 
ATOM   621  C CB    . LEU A 1 90  ? -40.756 -27.507 21.681  1.00 12.08 ? 90   LEU A CB    1 
ATOM   622  C CG    . LEU A 1 90  ? -40.310 -28.630 20.743  1.00 11.65 ? 90   LEU A CG    1 
ATOM   623  C CD1   . LEU A 1 90  ? -40.138 -29.956 21.475  1.00 11.96 ? 90   LEU A CD1   1 
ATOM   624  C CD2   . LEU A 1 90  ? -41.361 -28.739 19.637  1.00 12.55 ? 90   LEU A CD2   1 
ATOM   625  N N     . SER A 1 91  ? -37.440 -27.567 22.249  1.00 11.72 ? 91   SER A N     1 
ATOM   626  C CA    . SER A 1 91  ? -36.183 -27.401 21.550  1.00 11.82 ? 91   SER A CA    1 
ATOM   627  C C     . SER A 1 91  ? -36.162 -28.361 20.371  1.00 12.04 ? 91   SER A C     1 
ATOM   628  O O     . SER A 1 91  ? -36.185 -29.594 20.532  1.00 12.05 ? 91   SER A O     1 
ATOM   629  C CB    . SER A 1 91  ? -35.018 -27.621 22.483  1.00 11.97 ? 91   SER A CB    1 
ATOM   630  O OG    . SER A 1 91  ? -33.764 -27.567 21.823  1.00 12.09 ? 91   SER A OG    1 
ATOM   631  N N     . VAL A 1 92  ? -36.176 -27.770 19.171  1.00 10.99 ? 92   VAL A N     1 
ATOM   632  C CA    . VAL A 1 92  ? -36.185 -28.574 17.962  1.00 11.08 ? 92   VAL A CA    1 
ATOM   633  C C     . VAL A 1 92  ? -34.733 -28.704 17.501  1.00 10.94 ? 92   VAL A C     1 
ATOM   634  O O     . VAL A 1 92  ? -34.220 -27.818 16.847  1.00 11.55 ? 92   VAL A O     1 
ATOM   635  C CB    . VAL A 1 92  ? -37.088 -27.991 16.876  1.00 11.86 ? 92   VAL A CB    1 
ATOM   636  C CG1   . VAL A 1 92  ? -37.128 -28.927 15.669  1.00 11.55 ? 92   VAL A CG1   1 
ATOM   637  C CG2   . VAL A 1 92  ? -38.492 -27.749 17.434  1.00 12.44 ? 92   VAL A CG2   1 
ATOM   638  N N     . ASN A 1 93  ? -34.128 -29.839 17.816  1.00 11.24 ? 93   ASN A N     1 
ATOM   639  C CA    . ASN A 1 93  ? -32.712 -30.063 17.562  1.00 11.63 ? 93   ASN A CA    1 
ATOM   640  C C     . ASN A 1 93  ? -32.561 -30.561 16.122  1.00 12.53 ? 93   ASN A C     1 
ATOM   641  O O     . ASN A 1 93  ? -33.083 -31.635 15.806  1.00 13.56 ? 93   ASN A O     1 
ATOM   642  C CB    . ASN A 1 93  ? -32.150 -31.056 18.568  1.00 11.60 ? 93   ASN A CB    1 
ATOM   643  C CG    . ASN A 1 93  ? -30.655 -31.164 18.489  1.00 12.52 ? 93   ASN A CG    1 
ATOM   644  O OD1   . ASN A 1 93  ? -30.089 -31.236 17.392  1.00 12.68 ? 93   ASN A OD1   1 
ATOM   645  N ND2   . ASN A 1 93  ? -29.976 -31.163 19.639  1.00 12.38 ? 93   ASN A ND2   1 
ATOM   646  N N     . LEU A 1 94  ? -31.835 -29.793 15.285  1.00 11.08 ? 94   LEU A N     1 
ATOM   647  C CA    . LEU A 1 94  ? -31.776 -30.029 13.845  1.00 11.06 ? 94   LEU A CA    1 
ATOM   648  C C     . LEU A 1 94  ? -30.525 -30.807 13.463  1.00 11.75 ? 94   LEU A C     1 
ATOM   649  O O     . LEU A 1 94  ? -30.111 -30.774 12.306  1.00 11.32 ? 94   LEU A O     1 
ATOM   650  C CB    . LEU A 1 94  ? -31.843 -28.668 13.146  1.00 11.54 ? 94   LEU A CB    1 
ATOM   651  C CG    . LEU A 1 94  ? -33.143 -27.887 13.349  1.00 11.88 ? 94   LEU A CG    1 
ATOM   652  C CD1   . LEU A 1 94  ? -33.065 -26.503 12.741  1.00 11.05 ? 94   LEU A CD1   1 
ATOM   653  C CD2   . LEU A 1 94  ? -34.365 -28.592 12.822  1.00 12.93 ? 94   LEU A CD2   1 
ATOM   654  N N     . ASP A 1 95  ? -29.980 -31.607 14.393  1.00 11.57 ? 95   ASP A N     1 
ATOM   655  C CA    . ASP A 1 95  ? -28.716 -32.288 14.131  1.00 13.47 ? 95   ASP A CA    1 
ATOM   656  C C     . ASP A 1 95  ? -28.831 -33.259 12.946  1.00 13.88 ? 95   ASP A C     1 
ATOM   657  O O     . ASP A 1 95  ? -27.836 -33.531 12.283  1.00 14.81 ? 95   ASP A O     1 
ATOM   658  C CB    . ASP A 1 95  ? -28.313 -33.102 15.343  1.00 15.78 ? 95   ASP A CB    1 
ATOM   659  C CG    . ASP A 1 95  ? -26.937 -33.739 15.226  1.00 18.46 ? 95   ASP A CG    1 
ATOM   660  O OD1   . ASP A 1 95  ? -25.978 -32.993 14.969  1.00 19.66 ? 95   ASP A OD1   1 
ATOM   661  O OD2   . ASP A 1 95  ? -26.866 -34.996 15.295  1.00 23.49 ? 95   ASP A OD2   1 
ATOM   662  N N     . ASN A 1 96  ? -30.032 -33.798 12.681  1.00 13.93 ? 96   ASN A N     1 
ATOM   663  C CA    . ASN A 1 96  ? -30.182 -34.765 11.594  1.00 14.17 ? 96   ASN A CA    1 
ATOM   664  C C     . ASN A 1 96  ? -30.284 -34.092 10.216  1.00 16.08 ? 96   ASN A C     1 
ATOM   665  O O     . ASN A 1 96  ? -30.239 -34.794 9.195   1.00 16.35 ? 96   ASN A O     1 
ATOM   666  C CB    . ASN A 1 96  ? -31.405 -35.647 11.745  1.00 16.13 ? 96   ASN A CB    1 
ATOM   667  C CG    . ASN A 1 96  ? -31.276 -36.573 12.923  1.00 17.43 ? 96   ASN A CG    1 
ATOM   668  O OD1   . ASN A 1 96  ? -30.194 -37.097 13.201  1.00 20.81 ? 96   ASN A OD1   1 
ATOM   669  N ND2   . ASN A 1 96  ? -32.370 -36.761 13.638  1.00 18.06 ? 96   ASN A ND2   1 
ATOM   670  N N     . LEU A 1 97  ? -30.492 -32.765 10.156  1.00 13.43 ? 97   LEU A N     1 
ATOM   671  C CA    . LEU A 1 97  ? -30.714 -32.070 8.893   1.00 14.83 ? 97   LEU A CA    1 
ATOM   672  C C     . LEU A 1 97  ? -29.373 -31.569 8.360   1.00 14.28 ? 97   LEU A C     1 
ATOM   673  O O     . LEU A 1 97  ? -29.091 -30.365 8.424   1.00 14.74 ? 97   LEU A O     1 
ATOM   674  C CB    . LEU A 1 97  ? -31.697 -30.916 9.086   1.00 16.54 ? 97   LEU A CB    1 
ATOM   675  C CG    . LEU A 1 97  ? -33.187 -31.273 9.078   1.00 18.91 ? 97   LEU A CG    1 
ATOM   676  C CD1   . LEU A 1 97  ? -33.569 -32.067 10.295  1.00 22.36 ? 97   LEU A CD1   1 
ATOM   677  C CD2   . LEU A 1 97  ? -33.998 -30.006 9.016   1.00 19.15 ? 97   LEU A CD2   1 
ATOM   678  N N     . GLN A 1 98  ? -28.568 -32.500 7.870   1.00 14.14 ? 98   GLN A N     1 
ATOM   679  C CA    . GLN A 1 98  ? -27.202 -32.200 7.447   1.00 15.41 ? 98   GLN A CA    1 
ATOM   680  C C     . GLN A 1 98  ? -26.950 -32.584 5.998   1.00 15.53 ? 98   GLN A C     1 
ATOM   681  O O     . GLN A 1 98  ? -25.814 -32.849 5.590   1.00 16.15 ? 98   GLN A O     1 
ATOM   682  C CB    . GLN A 1 98  ? -26.147 -32.905 8.280   1.00 15.85 ? 98   GLN A CB    1 
ATOM   683  C CG    . GLN A 1 98  ? -26.207 -32.462 9.722   1.00 17.92 ? 98   GLN A CG    1 
ATOM   684  C CD    . GLN A 1 98  ? -24.938 -32.733 10.494  1.00 17.76 ? 98   GLN A CD    1 
ATOM   685  O OE1   . GLN A 1 98  ? -23.820 -32.697 9.956   1.00 18.40 ? 98   GLN A OE1   1 
ATOM   686  N NE2   . GLN A 1 98  ? -25.110 -33.051 11.766  1.00 19.32 ? 98   GLN A NE2   1 
ATOM   687  N N     . HIS A 1 99  ? -27.988 -32.569 5.182   1.00 15.54 ? 99   HIS A N     1 
ATOM   688  C CA    . HIS A 1 99  ? -27.761 -32.854 3.784   1.00 16.05 ? 99   HIS A CA    1 
ATOM   689  C C     . HIS A 1 99  ? -26.903 -31.759 3.140   1.00 15.45 ? 99   HIS A C     1 
ATOM   690  O O     . HIS A 1 99  ? -26.806 -30.616 3.598   1.00 12.25 ? 99   HIS A O     1 
ATOM   691  C CB    . HIS A 1 99  ? -29.094 -33.062 3.083   1.00 18.35 ? 99   HIS A CB    1 
ATOM   692  C CG    . HIS A 1 99  ? -29.570 -31.888 2.368   1.00 21.89 ? 99   HIS A CG    1 
ATOM   693  N ND1   . HIS A 1 99  ? -30.359 -30.908 2.912   1.00 27.16 ? 99   HIS A ND1   1 
ATOM   694  C CD2   . HIS A 1 99  ? -29.347 -31.565 1.075   1.00 26.74 ? 99   HIS A CD2   1 
ATOM   695  C CE1   . HIS A 1 99  ? -30.592 -29.987 1.976   1.00 25.83 ? 99   HIS A CE1   1 
ATOM   696  N NE2   . HIS A 1 99  ? -29.985 -30.375 0.853   1.00 29.85 ? 99   HIS A NE2   1 
ATOM   697  N N     . PHE A 1 100 ? -26.265 -32.164 2.048   1.00 15.47 ? 100  PHE A N     1 
ATOM   698  C CA    . PHE A 1 100 ? -25.411 -31.276 1.275   1.00 14.67 ? 100  PHE A CA    1 
ATOM   699  C C     . PHE A 1 100 ? -25.406 -31.781 -0.160  1.00 15.47 ? 100  PHE A C     1 
ATOM   700  O O     . PHE A 1 100 ? -25.150 -32.956 -0.407  1.00 16.02 ? 100  PHE A O     1 
ATOM   701  C CB    . PHE A 1 100 ? -23.974 -31.247 1.772   1.00 13.73 ? 100  PHE A CB    1 
ATOM   702  C CG    . PHE A 1 100 ? -23.080 -30.279 0.992   1.00 15.15 ? 100  PHE A CG    1 
ATOM   703  C CD1   . PHE A 1 100 ? -22.519 -30.633 -0.223  1.00 16.61 ? 100  PHE A CD1   1 
ATOM   704  C CD2   . PHE A 1 100 ? -22.802 -29.020 1.506   1.00 14.45 ? 100  PHE A CD2   1 
ATOM   705  C CE1   . PHE A 1 100 ? -21.738 -29.718 -0.939  1.00 15.82 ? 100  PHE A CE1   1 
ATOM   706  C CE2   . PHE A 1 100 ? -22.009 -28.121 0.807   1.00 15.46 ? 100  PHE A CE2   1 
ATOM   707  C CZ    . PHE A 1 100 ? -21.500 -28.450 -0.419  1.00 16.17 ? 100  PHE A CZ    1 
ATOM   708  N N     . SER A 1 101 ? -25.688 -30.879 -1.088  1.00 15.63 ? 101  SER A N     1 
ATOM   709  C CA    . SER A 1 101 ? -25.531 -31.177 -2.499  1.00 16.15 ? 101  SER A CA    1 
ATOM   710  C C     . SER A 1 101 ? -25.079 -29.908 -3.217  1.00 17.03 ? 101  SER A C     1 
ATOM   711  O O     . SER A 1 101 ? -25.297 -28.793 -2.744  1.00 17.15 ? 101  SER A O     1 
ATOM   712  C CB    . SER A 1 101 ? -26.783 -31.764 -3.064  1.00 18.95 ? 101  SER A CB    1 
ATOM   713  O OG    . SER A 1 101 ? -27.799 -30.790 -3.126  1.00 21.03 ? 101  SER A OG    1 
ATOM   714  N N     . MET A 1 102 ? -24.303 -30.082 -4.284  1.00 16.00 ? 102  MET A N     1 
ATOM   715  C CA    . MET A 1 102 ? -23.738 -28.963 -5.027  1.00 15.72 ? 102  MET A CA    1 
ATOM   716  C C     . MET A 1 102 ? -24.299 -28.991 -6.450  1.00 16.52 ? 102  MET A C     1 
ATOM   717  O O     . MET A 1 102 ? -24.224 -30.018 -7.146  1.00 18.20 ? 102  MET A O     1 
ATOM   718  C CB    . MET A 1 102 ? -22.198 -29.058 -5.069  1.00 14.60 ? 102  MET A CB    1 
ATOM   719  C CG    . MET A 1 102 ? -21.549 -27.940 -5.827  1.00 15.03 ? 102  MET A CG    1 
ATOM   720  S SD    . MET A 1 102 ? -21.732 -26.280 -5.158  1.00 16.62 ? 102  MET A SD    1 
ATOM   721  C CE    . MET A 1 102 ? -20.481 -26.329 -3.870  1.00 15.46 ? 102  MET A CE    1 
ATOM   722  N N     . ASN A 1 103 ? -24.878 -27.911 -6.870  1.00 17.54 ? 103  ASN A N     1 
ATOM   723  C CA    . ASN A 1 103 ? -25.281 -27.676 -8.250  1.00 18.72 ? 103  ASN A CA    1 
ATOM   724  C C     . ASN A 1 103 ? -24.047 -27.171 -9.006  1.00 19.28 ? 103  ASN A C     1 
ATOM   725  O O     . ASN A 1 103 ? -23.665 -25.998 -8.849  1.00 18.39 ? 103  ASN A O     1 
ATOM   726  C CB    . ASN A 1 103 ? -26.440 -26.682 -8.342  1.00 30.00 ? 103  ASN A CB    1 
ATOM   727  C CG    . ASN A 1 103 ? -26.970 -26.532 -9.754  1.00 30.00 ? 103  ASN A CG    1 
ATOM   728  O OD1   . ASN A 1 103 ? -26.287 -26.860 -10.724 1.00 30.00 ? 103  ASN A OD1   1 
ATOM   729  N ND2   . ASN A 1 103 ? -28.195 -26.035 -9.877  1.00 30.00 ? 103  ASN A ND2   1 
ATOM   730  N N     . GLU A 1 104 ? -23.426 -27.981 -9.766  1.00 19.81 ? 104  GLU A N     1 
ATOM   731  C CA    . GLU A 1 104 ? -22.150 -27.604 -10.367 1.00 21.90 ? 104  GLU A CA    1 
ATOM   732  C C     . GLU A 1 104 ? -22.333 -26.637 -11.532 1.00 22.52 ? 104  GLU A C     1 
ATOM   733  O O     . GLU A 1 104 ? -21.381 -25.976 -11.925 1.00 21.78 ? 104  GLU A O     1 
ATOM   734  C CB    . GLU A 1 104 ? -21.288 -28.784 -10.812 1.00 24.55 ? 104  GLU A CB    1 
ATOM   735  C CG    . GLU A 1 104 ? -21.055 -29.809 -9.701  1.00 29.88 ? 104  GLU A CG    1 
ATOM   736  C CD    . GLU A 1 104 ? -22.208 -30.768 -9.364  1.00 35.07 ? 104  GLU A CD    1 
ATOM   737  O OE1   . GLU A 1 104 ? -22.026 -31.553 -8.351  1.00 32.30 ? 104  GLU A OE1   1 
ATOM   738  O OE2   . GLU A 1 104 ? -23.268 -30.742 -10.103 1.00 35.39 ? 104  GLU A OE2   1 
ATOM   739  N N     . THR A 1 105 ? -23.561 -26.489 -12.046 1.00 22.75 ? 105  THR A N     1 
ATOM   740  C CA    . THR A 1 105 ? -23.777 -25.483 -13.077 1.00 25.89 ? 105  THR A CA    1 
ATOM   741  C C     . THR A 1 105 ? -23.553 -24.062 -12.574 1.00 26.83 ? 105  THR A C     1 
ATOM   742  O O     . THR A 1 105 ? -23.026 -23.226 -13.306 1.00 27.76 ? 105  THR A O     1 
ATOM   743  C CB    . THR A 1 105 ? -25.178 -25.560 -13.660 1.00 27.89 ? 105  THR A CB    1 
ATOM   744  O OG1   . THR A 1 105 ? -25.237 -26.903 -14.105 1.00 32.49 ? 105  THR A OG1   1 
ATOM   745  C CG2   . THR A 1 105 ? -25.305 -24.564 -14.793 1.00 31.46 ? 105  THR A CG2   1 
ATOM   746  N N     . SER A 1 106 ? -24.011 -23.775 -11.349 1.00 22.02 ? 106  SER A N     1 
ATOM   747  C CA    . SER A 1 106 ? -23.883 -22.446 -10.781 1.00 20.02 ? 106  SER A CA    1 
ATOM   748  C C     . SER A 1 106 ? -22.920 -22.434 -9.593  1.00 19.75 ? 106  SER A C     1 
ATOM   749  O O     . SER A 1 106 ? -22.580 -21.367 -9.101  1.00 21.98 ? 106  SER A O     1 
ATOM   750  C CB    . SER A 1 106 ? -25.207 -21.939 -10.379 1.00 19.83 ? 106  SER A CB    1 
ATOM   751  O OG    . SER A 1 106 ? -25.800 -22.888 -9.519  1.00 19.39 ? 106  SER A OG    1 
ATOM   752  N N     . TRP A 1 107 ? -22.512 -23.610 -9.138  1.00 15.53 ? 107  TRP A N     1 
ATOM   753  C CA    . TRP A 1 107 ? -21.827 -23.765 -7.866  1.00 16.43 ? 107  TRP A CA    1 
ATOM   754  C C     . TRP A 1 107 ? -22.675 -23.205 -6.719  1.00 16.74 ? 107  TRP A C     1 
ATOM   755  O O     . TRP A 1 107 ? -22.175 -22.568 -5.787  1.00 16.99 ? 107  TRP A O     1 
ATOM   756  C CB    . TRP A 1 107 ? -20.435 -23.134 -7.880  1.00 18.16 ? 107  TRP A CB    1 
ATOM   757  C CG    . TRP A 1 107 ? -19.491 -23.728 -8.897  1.00 15.96 ? 107  TRP A CG    1 
ATOM   758  C CD1   . TRP A 1 107 ? -18.943 -23.076 -9.955  1.00 20.18 ? 107  TRP A CD1   1 
ATOM   759  C CD2   . TRP A 1 107 ? -19.055 -25.092 -8.997  1.00 16.29 ? 107  TRP A CD2   1 
ATOM   760  N NE1   . TRP A 1 107 ? -18.150 -23.925 -10.685 1.00 18.75 ? 107  TRP A NE1   1 
ATOM   761  C CE2   . TRP A 1 107 ? -18.174 -25.157 -10.098 1.00 16.74 ? 107  TRP A CE2   1 
ATOM   762  C CE3   . TRP A 1 107 ? -19.234 -26.238 -8.222  1.00 16.42 ? 107  TRP A CE3   1 
ATOM   763  C CZ2   . TRP A 1 107 ? -17.548 -26.341 -10.457 1.00 16.12 ? 107  TRP A CZ2   1 
ATOM   764  C CZ3   . TRP A 1 107 ? -18.620 -27.411 -8.572  1.00 16.27 ? 107  TRP A CZ3   1 
ATOM   765  C CH2   . TRP A 1 107 ? -17.774 -27.455 -9.693  1.00 14.69 ? 107  TRP A CH2   1 
ATOM   766  N N     . THR A 1 108 ? -23.968 -23.494 -6.757  1.00 15.76 ? 108  THR A N     1 
ATOM   767  C CA    . THR A 1 108 ? -24.842 -23.184 -5.635  1.00 15.33 ? 108  THR A CA    1 
ATOM   768  C C     . THR A 1 108 ? -25.077 -24.473 -4.855  1.00 14.67 ? 108  THR A C     1 
ATOM   769  O O     . THR A 1 108 ? -25.484 -25.482 -5.426  1.00 14.91 ? 108  THR A O     1 
ATOM   770  C CB    . THR A 1 108 ? -26.140 -22.589 -6.153  1.00 18.51 ? 108  THR A CB    1 
ATOM   771  O OG1   . THR A 1 108 ? -25.785 -21.403 -6.864  1.00 20.03 ? 108  THR A OG1   1 
ATOM   772  C CG2   . THR A 1 108 ? -27.105 -22.254 -5.035  1.00 17.24 ? 108  THR A CG2   1 
ATOM   773  N N     . ALA A 1 109 ? -24.838 -24.415 -3.542  1.00 13.61 ? 109  ALA A N     1 
ATOM   774  C CA    . ALA A 1 109 ? -24.938 -25.571 -2.669  1.00 13.49 ? 109  ALA A CA    1 
ATOM   775  C C     . ALA A 1 109 ? -26.318 -25.542 -2.021  1.00 13.87 ? 109  ALA A C     1 
ATOM   776  O O     . ALA A 1 109 ? -26.873 -24.467 -1.746  1.00 12.71 ? 109  ALA A O     1 
ATOM   777  C CB    . ALA A 1 109 ? -23.860 -25.518 -1.626  1.00 14.11 ? 109  ALA A CB    1 
ATOM   778  N N     . ARG A 1 110 ? -26.849 -26.723 -1.754  1.00 14.08 ? 110  ARG A N     1 
ATOM   779  C CA    . ARG A 1 110 ? -28.066 -26.857 -0.977  1.00 15.58 ? 110  ARG A CA    1 
ATOM   780  C C     . ARG A 1 110 ? -27.733 -27.590 0.306   1.00 15.78 ? 110  ARG A C     1 
ATOM   781  O O     . ARG A 1 110 ? -27.140 -28.640 0.241   1.00 18.66 ? 110  ARG A O     1 
ATOM   782  C CB    . ARG A 1 110 ? -29.016 -27.696 -1.825  1.00 20.45 ? 110  ARG A CB    1 
ATOM   783  C CG    . ARG A 1 110 ? -30.431 -27.574 -1.322  1.00 27.84 ? 110  ARG A CG    1 
ATOM   784  C CD    . ARG A 1 110 ? -31.337 -28.080 -2.418  1.00 30.29 ? 110  ARG A CD    1 
ATOM   785  N NE    . ARG A 1 110 ? -32.529 -28.582 -1.755  1.00 31.05 ? 110  ARG A NE    1 
ATOM   786  C CZ    . ARG A 1 110 ? -33.460 -29.263 -2.390  1.00 41.32 ? 110  ARG A CZ    1 
ATOM   787  N NH1   . ARG A 1 110 ? -33.314 -29.533 -3.683  1.00 36.59 ? 110  ARG A NH1   1 
ATOM   788  N NH2   . ARG A 1 110 ? -34.524 -29.672 -1.716  1.00 45.62 ? 110  ARG A NH2   1 
ATOM   789  N N     . LEU A 1 111 ? -28.062 -27.020 1.467   1.00 15.02 ? 111  LEU A N     1 
ATOM   790  C CA    . LEU A 1 111 ? -27.491 -27.515 2.707   1.00 15.09 ? 111  LEU A CA    1 
ATOM   791  C C     . LEU A 1 111 ? -28.554 -27.432 3.800   1.00 12.94 ? 111  LEU A C     1 
ATOM   792  O O     . LEU A 1 111 ? -29.194 -26.394 3.951   1.00 14.29 ? 111  LEU A O     1 
ATOM   793  C CB    . LEU A 1 111 ? -26.314 -26.727 3.287   1.00 18.05 ? 111  LEU A CB    1 
ATOM   794  C CG    . LEU A 1 111 ? -25.218 -26.166 2.411   1.00 20.79 ? 111  LEU A CG    1 
ATOM   795  C CD1   . LEU A 1 111 ? -25.654 -24.878 1.762   1.00 20.47 ? 111  LEU A CD1   1 
ATOM   796  C CD2   . LEU A 1 111 ? -24.015 -26.004 3.340   1.00 17.68 ? 111  LEU A CD2   1 
ATOM   797  N N     . GLY A 1 112 ? -28.554 -28.435 4.675   1.00 11.74 ? 112  GLY A N     1 
ATOM   798  C CA    . GLY A 1 112 ? -29.403 -28.414 5.843   1.00 12.45 ? 112  GLY A CA    1 
ATOM   799  C C     . GLY A 1 112 ? -28.809 -27.572 6.983   1.00 11.72 ? 112  GLY A C     1 
ATOM   800  O O     . GLY A 1 112 ? -27.592 -27.394 7.113   1.00 11.65 ? 112  GLY A O     1 
ATOM   801  N N     . PRO A 1 113 ? -29.663 -27.090 7.898   1.00 12.52 ? 113  PRO A N     1 
ATOM   802  C CA    . PRO A 1 113 ? -29.236 -26.236 9.016   1.00 12.29 ? 113  PRO A CA    1 
ATOM   803  C C     . PRO A 1 113 ? -28.297 -26.892 10.025  1.00 11.47 ? 113  PRO A C     1 
ATOM   804  O O     . PRO A 1 113 ? -27.590 -26.193 10.739  1.00 11.39 ? 113  PRO A O     1 
ATOM   805  C CB    . PRO A 1 113 ? -30.577 -25.784 9.655   1.00 12.56 ? 113  PRO A CB    1 
ATOM   806  C CG    . PRO A 1 113 ? -31.518 -26.925 9.295   1.00 13.00 ? 113  PRO A CG    1 
ATOM   807  C CD    . PRO A 1 113 ? -31.118 -27.228 7.844   1.00 13.26 ? 113  PRO A CD    1 
ATOM   808  N N     . GLY A 1 114 ? -28.349 -28.221 10.123  1.00 11.00 ? 114  GLY A N     1 
ATOM   809  C CA    . GLY A 1 114 ? -27.542 -28.972 11.084  1.00 11.57 ? 114  GLY A CA    1 
ATOM   810  C C     . GLY A 1 114 ? -26.080 -29.081 10.702  1.00 11.71 ? 114  GLY A C     1 
ATOM   811  O O     . GLY A 1 114 ? -25.284 -29.484 11.533  1.00 11.71 ? 114  GLY A O     1 
ATOM   812  N N     . ASN A 1 115 ? -25.730 -28.703 9.460   1.00 11.66 ? 115  ASN A N     1 
ATOM   813  C CA    . ASN A 1 115 ? -24.329 -28.686 9.074   1.00 12.20 ? 115  ASN A CA    1 
ATOM   814  C C     . ASN A 1 115 ? -23.589 -27.700 9.953   1.00 11.54 ? 115  ASN A C     1 
ATOM   815  O O     . ASN A 1 115 ? -23.975 -26.546 10.037  1.00 12.26 ? 115  ASN A O     1 
ATOM   816  C CB    . ASN A 1 115 ? -24.139 -28.260 7.631   1.00 11.97 ? 115  ASN A CB    1 
ATOM   817  C CG    . ASN A 1 115 ? -24.511 -29.352 6.665   1.00 12.22 ? 115  ASN A CG    1 
ATOM   818  O OD1   . ASN A 1 115 ? -23.748 -30.299 6.523   1.00 15.04 ? 115  ASN A OD1   1 
ATOM   819  N ND2   . ASN A 1 115 ? -25.641 -29.228 5.981   1.00 11.91 ? 115  ASN A ND2   1 
ATOM   820  N N     . ARG A 1 116 ? -22.487 -28.139 10.575  1.00 11.89 ? 116  ARG A N     1 
ATOM   821  C CA    . ARG A 1 116 ? -21.604 -27.213 11.268  1.00 12.19 ? 116  ARG A CA    1 
ATOM   822  C C     . ARG A 1 116 ? -20.600 -26.624 10.275  1.00 12.22 ? 116  ARG A C     1 
ATOM   823  O O     . ARG A 1 116 ? -20.434 -27.158 9.185   1.00 11.82 ? 116  ARG A O     1 
ATOM   824  C CB    . ARG A 1 116 ? -20.839 -27.890 12.408  1.00 13.01 ? 116  ARG A CB    1 
ATOM   825  C CG    . ARG A 1 116 ? -21.594 -27.938 13.723  1.00 15.92 ? 116  ARG A CG    1 
ATOM   826  C CD    . ARG A 1 116 ? -22.903 -28.628 13.659  1.00 17.10 ? 116  ARG A CD    1 
ATOM   827  N NE    . ARG A 1 116 ? -23.363 -28.977 15.023  1.00 16.96 ? 116  ARG A NE    1 
ATOM   828  C CZ    . ARG A 1 116 ? -24.370 -29.834 15.248  1.00 20.84 ? 116  ARG A CZ    1 
ATOM   829  N NH1   . ARG A 1 116 ? -25.084 -30.338 14.244  1.00 20.81 ? 116  ARG A NH1   1 
ATOM   830  N NH2   . ARG A 1 116 ? -24.638 -30.221 16.489  1.00 19.40 ? 116  ARG A NH2   1 
ATOM   831  N N     . LEU A 1 117 ? -20.000 -25.478 10.610  1.00 11.76 ? 117  LEU A N     1 
ATOM   832  C CA    . LEU A 1 117 ? -19.214 -24.745 9.628   1.00 11.72 ? 117  LEU A CA    1 
ATOM   833  C C     . LEU A 1 117 ? -18.010 -25.550 9.127   1.00 11.30 ? 117  LEU A C     1 
ATOM   834  O O     . LEU A 1 117 ? -17.569 -25.354 7.994   1.00 12.46 ? 117  LEU A O     1 
ATOM   835  C CB    . LEU A 1 117 ? -18.749 -23.405 10.178  1.00 12.94 ? 117  LEU A CB    1 
ATOM   836  C CG    . LEU A 1 117 ? -19.833 -22.351 10.401  1.00 16.20 ? 117  LEU A CG    1 
ATOM   837  C CD1   . LEU A 1 117 ? -19.259 -21.025 10.828  1.00 17.90 ? 117  LEU A CD1   1 
ATOM   838  C CD2   . LEU A 1 117 ? -20.724 -22.165 9.188   1.00 16.53 ? 117  LEU A CD2   1 
ATOM   839  N N     . GLY A 1 118 ? -17.427 -26.426 9.952   1.00 11.70 ? 118  GLY A N     1 
ATOM   840  C CA    . GLY A 1 118 ? -16.327 -27.266 9.503   1.00 11.58 ? 118  GLY A CA    1 
ATOM   841  C C     . GLY A 1 118 ? -16.765 -28.197 8.366   1.00 12.73 ? 118  GLY A C     1 
ATOM   842  O O     . GLY A 1 118 ? -16.091 -28.302 7.337   1.00 12.66 ? 118  GLY A O     1 
ATOM   843  N N     . ARG A 1 119 ? -17.920 -28.829 8.494   1.00 12.98 ? 119  ARG A N     1 
ATOM   844  C CA    . ARG A 1 119 ? -18.469 -29.621 7.390   1.00 13.37 ? 119  ARG A CA    1 
ATOM   845  C C     . ARG A 1 119 ? -18.829 -28.768 6.165   1.00 13.35 ? 119  ARG A C     1 
ATOM   846  O O     . ARG A 1 119 ? -18.618 -29.169 5.015   1.00 14.31 ? 119  ARG A O     1 
ATOM   847  C CB    . ARG A 1 119 ? -19.743 -30.316 7.872   1.00 13.94 ? 119  ARG A CB    1 
ATOM   848  C CG    . ARG A 1 119 ? -20.357 -31.305 6.898   1.00 15.68 ? 119  ARG A CG    1 
ATOM   849  C CD    . ARG A 1 119 ? -21.418 -32.156 7.568   1.00 17.34 ? 119  ARG A CD    1 
ATOM   850  N NE    . ARG A 1 119 ? -22.409 -32.663 6.625   1.00 18.21 ? 119  ARG A NE    1 
ATOM   851  C CZ    . ARG A 1 119 ? -22.334 -33.749 5.888   1.00 19.71 ? 119  ARG A CZ    1 
ATOM   852  N NH1   . ARG A 1 119 ? -21.282 -34.544 5.943   1.00 21.44 ? 119  ARG A NH1   1 
ATOM   853  N NH2   . ARG A 1 119 ? -23.330 -34.059 5.097   1.00 21.91 ? 119  ARG A NH2   1 
ATOM   854  N N     . VAL A 1 120 ? -19.431 -27.597 6.385   1.00 12.83 ? 120  VAL A N     1 
ATOM   855  C CA    . VAL A 1 120 ? -19.764 -26.684 5.285   1.00 12.58 ? 120  VAL A CA    1 
ATOM   856  C C     . VAL A 1 120 ? -18.486 -26.371 4.514   1.00 12.74 ? 120  VAL A C     1 
ATOM   857  O O     . VAL A 1 120 ? -18.457 -26.506 3.279   1.00 12.96 ? 120  VAL A O     1 
ATOM   858  C CB    . VAL A 1 120 ? -20.411 -25.370 5.731   1.00 13.38 ? 120  VAL A CB    1 
ATOM   859  C CG1   . VAL A 1 120 ? -20.518 -24.380 4.574   1.00 14.85 ? 120  VAL A CG1   1 
ATOM   860  C CG2   . VAL A 1 120 ? -21.766 -25.633 6.394   1.00 13.41 ? 120  VAL A CG2   1 
ATOM   861  N N     . THR A 1 121 ? -17.430 -26.010 5.252   1.00 12.44 ? 121  THR A N     1 
ATOM   862  C CA    . THR A 1 121 ? -16.159 -25.632 4.633   1.00 12.70 ? 121  THR A CA    1 
ATOM   863  C C     . THR A 1 121 ? -15.543 -26.800 3.864   1.00 12.93 ? 121  THR A C     1 
ATOM   864  O O     . THR A 1 121 ? -15.103 -26.619 2.714   1.00 12.97 ? 121  THR A O     1 
ATOM   865  C CB    . THR A 1 121 ? -15.191 -25.085 5.693   1.00 14.31 ? 121  THR A CB    1 
ATOM   866  O OG1   . THR A 1 121 ? -15.847 -23.987 6.328   1.00 14.36 ? 121  THR A OG1   1 
ATOM   867  C CG2   . THR A 1 121 ? -13.903 -24.618 5.057   1.00 15.23 ? 121  THR A CG2   1 
ATOM   868  N N     . GLU A 1 122 ? -15.498 -27.985 4.488   1.00 12.80 ? 122  GLU A N     1 
ATOM   869  C CA    . GLU A 1 122 ? -14.928 -29.167 3.861   1.00 13.68 ? 122  GLU A CA    1 
ATOM   870  C C     . GLU A 1 122 ? -15.672 -29.546 2.576   1.00 14.16 ? 122  GLU A C     1 
ATOM   871  O O     . GLU A 1 122 ? -15.075 -29.811 1.515   1.00 13.84 ? 122  GLU A O     1 
ATOM   872  C CB    . GLU A 1 122 ? -14.977 -30.344 4.837   1.00 16.66 ? 122  GLU A CB    1 
ATOM   873  C CG    . GLU A 1 122 ? -14.336 -31.618 4.277   1.00 21.15 ? 122  GLU A CG    1 
ATOM   874  C CD    . GLU A 1 122 ? -14.087 -32.665 5.350   1.00 27.95 ? 122  GLU A CD    1 
ATOM   875  O OE1   . GLU A 1 122 ? -13.001 -33.274 5.365   1.00 37.80 ? 122  GLU A OE1   1 
ATOM   876  O OE2   . GLU A 1 122 ? -14.951 -32.791 6.235   1.00 34.50 ? 122  GLU A OE2   1 
ATOM   877  N N     . LEU A 1 123 ? -17.004 -29.600 2.665   1.00 12.90 ? 123  LEU A N     1 
ATOM   878  C CA    . LEU A 1 123 ? -17.812 -30.061 1.544   1.00 13.69 ? 123  LEU A CA    1 
ATOM   879  C C     . LEU A 1 123 ? -17.841 -29.053 0.414   1.00 15.55 ? 123  LEU A C     1 
ATOM   880  O O     . LEU A 1 123 ? -17.832 -29.448 -0.785  1.00 13.42 ? 123  LEU A O     1 
ATOM   881  C CB    . LEU A 1 123 ? -19.216 -30.445 1.997   1.00 13.82 ? 123  LEU A CB    1 
ATOM   882  C CG    . LEU A 1 123 ? -19.247 -31.696 2.870   1.00 14.35 ? 123  LEU A CG    1 
ATOM   883  C CD1   . LEU A 1 123 ? -20.706 -31.984 3.122   1.00 16.22 ? 123  LEU A CD1   1 
ATOM   884  C CD2   . LEU A 1 123 ? -18.553 -32.873 2.228   1.00 17.91 ? 123  LEU A CD2   1 
ATOM   885  N N     . MET A 1 124 ? -17.808 -27.750 0.723   1.00 11.68 ? 124  MET A N     1 
ATOM   886  C CA    . MET A 1 124 ? -17.754 -26.767 -0.343  1.00 12.12 ? 124  MET A CA    1 
ATOM   887  C C     . MET A 1 124 ? -16.409 -26.843 -1.070  1.00 11.91 ? 124  MET A C     1 
ATOM   888  O O     . MET A 1 124 ? -16.369 -26.734 -2.294  1.00 11.45 ? 124  MET A O     1 
ATOM   889  C CB    . MET A 1 124 ? -17.989 -25.351 0.184   1.00 12.25 ? 124  MET A CB    1 
ATOM   890  C CG    . MET A 1 124 ? -19.476 -25.078 0.458   1.00 12.77 ? 124  MET A CG    1 
ATOM   891  S SD    . MET A 1 124 ? -19.685 -23.340 0.857   1.00 14.48 ? 124  MET A SD    1 
ATOM   892  C CE    . MET A 1 124 ? -21.468 -23.236 1.025   1.00 14.74 ? 124  MET A CE    1 
ATOM   893  N N     . TYR A 1 125 ? -15.326 -27.012 -0.308  1.00 11.22 ? 125  TYR A N     1 
ATOM   894  C CA    . TYR A 1 125 ? -14.004 -27.148 -0.911  1.00 12.00 ? 125  TYR A CA    1 
ATOM   895  C C     . TYR A 1 125 ? -13.958 -28.395 -1.786  1.00 12.36 ? 125  TYR A C     1 
ATOM   896  O O     . TYR A 1 125 ? -13.466 -28.359 -2.926  1.00 12.94 ? 125  TYR A O     1 
ATOM   897  C CB    . TYR A 1 125 ? -12.885 -27.173 0.138   1.00 11.29 ? 125  TYR A CB    1 
ATOM   898  C CG    . TYR A 1 125 ? -11.525 -27.296 -0.534  1.00 13.20 ? 125  TYR A CG    1 
ATOM   899  C CD1   . TYR A 1 125 ? -10.970 -26.225 -1.232  1.00 15.68 ? 125  TYR A CD1   1 
ATOM   900  C CD2   . TYR A 1 125 ? -10.855 -28.506 -0.558  1.00 13.39 ? 125  TYR A CD2   1 
ATOM   901  C CE1   . TYR A 1 125 ? -9.755  -26.382 -1.892  1.00 17.06 ? 125  TYR A CE1   1 
ATOM   902  C CE2   . TYR A 1 125 ? -9.632  -28.668 -1.197  1.00 14.13 ? 125  TYR A CE2   1 
ATOM   903  C CZ    . TYR A 1 125 ? -9.079  -27.595 -1.859  1.00 17.05 ? 125  TYR A CZ    1 
ATOM   904  O OH    . TYR A 1 125 ? -7.876  -27.809 -2.518  1.00 17.67 ? 125  TYR A OH    1 
ATOM   905  N N     . ASN A 1 126 ? -14.412 -29.519 -1.253  1.00 10.85 ? 126  ASN A N     1 
ATOM   906  C CA    . ASN A 1 126 ? -14.309 -30.779 -1.980  1.00 12.35 ? 126  ASN A CA    1 
ATOM   907  C C     . ASN A 1 126 ? -15.145 -30.790 -3.258  1.00 13.18 ? 126  ASN A C     1 
ATOM   908  O O     . ASN A 1 126 ? -14.806 -31.518 -4.195  1.00 13.11 ? 126  ASN A O     1 
ATOM   909  C CB    . ASN A 1 126 ? -14.679 -31.914 -1.052  1.00 14.70 ? 126  ASN A CB    1 
ATOM   910  C CG    . ASN A 1 126 ? -13.615 -32.167 0.004   1.00 17.23 ? 126  ASN A CG    1 
ATOM   911  O OD1   . ASN A 1 126 ? -12.529 -31.577 -0.003  1.00 22.52 ? 126  ASN A OD1   1 
ATOM   912  N ND2   . ASN A 1 126 ? -13.889 -33.089 0.897   1.00 21.90 ? 126  ASN A ND2   1 
ATOM   913  N N     . ASN A 1 127 ? -16.275 -30.067 -3.273  1.00 12.85 ? 127  ASN A N     1 
ATOM   914  C CA    . ASN A 1 127 ? -17.165 -29.996 -4.415  1.00 12.79 ? 127  ASN A CA    1 
ATOM   915  C C     . ASN A 1 127 ? -16.785 -28.833 -5.311  1.00 13.20 ? 127  ASN A C     1 
ATOM   916  O O     . ASN A 1 127 ? -17.504 -27.838 -5.375  1.00 14.67 ? 127  ASN A O     1 
ATOM   917  C CB    . ASN A 1 127 ? -18.621 -29.933 -3.952  1.00 13.24 ? 127  ASN A CB    1 
ATOM   918  C CG    . ASN A 1 127 ? -19.069 -31.292 -3.473  1.00 15.07 ? 127  ASN A CG    1 
ATOM   919  O OD1   . ASN A 1 127 ? -19.506 -32.117 -4.294  1.00 15.85 ? 127  ASN A OD1   1 
ATOM   920  N ND2   . ASN A 1 127 ? -18.948 -31.565 -2.178  1.00 15.49 ? 127  ASN A ND2   1 
ATOM   921  N N     . GLY A 1 128 ? -15.609 -28.916 -5.961  1.00 13.16 ? 128  GLY A N     1 
ATOM   922  C CA    . GLY A 1 128 ? -15.246 -27.937 -6.970  1.00 14.73 ? 128  GLY A CA    1 
ATOM   923  C C     . GLY A 1 128 ? -14.397 -26.768 -6.462  1.00 14.25 ? 128  GLY A C     1 
ATOM   924  O O     . GLY A 1 128 ? -14.161 -25.827 -7.213  1.00 14.70 ? 128  GLY A O     1 
ATOM   925  N N     . GLY A 1 129 ? -13.862 -26.867 -5.245  1.00 12.34 ? 129  GLY A N     1 
ATOM   926  C CA    . GLY A 1 129 ? -12.937 -25.859 -4.752  1.00 11.85 ? 129  GLY A CA    1 
ATOM   927  C C     . GLY A 1 129 ? -13.634 -24.546 -4.412  1.00 12.30 ? 129  GLY A C     1 
ATOM   928  O O     . GLY A 1 129 ? -13.146 -23.455 -4.717  1.00 11.42 ? 129  GLY A O     1 
ATOM   929  N N     . ARG A 1 130 ? -14.776 -24.652 -3.721  1.00 12.98 ? 130  ARG A N     1 
ATOM   930  C CA    . ARG A 1 130 ? -15.596 -23.480 -3.416  1.00 13.19 ? 130  ARG A CA    1 
ATOM   931  C C     . ARG A 1 130 ? -15.575 -23.115 -1.932  1.00 12.43 ? 130  ARG A C     1 
ATOM   932  O O     . ARG A 1 130 ? -15.198 -23.920 -1.079  1.00 11.54 ? 130  ARG A O     1 
ATOM   933  C CB    . ARG A 1 130 ? -17.046 -23.747 -3.823  1.00 12.41 ? 130  ARG A CB    1 
ATOM   934  C CG    . ARG A 1 130 ? -17.233 -24.411 -5.186  1.00 13.23 ? 130  ARG A CG    1 
ATOM   935  C CD    . ARG A 1 130 ? -16.685 -23.587 -6.325  1.00 12.54 ? 130  ARG A CD    1 
ATOM   936  N NE    . ARG A 1 130 ? -17.450 -22.359 -6.498  1.00 12.26 ? 130  ARG A NE    1 
ATOM   937  C CZ    . ARG A 1 130 ? -17.283 -21.487 -7.478  1.00 13.91 ? 130  ARG A CZ    1 
ATOM   938  N NH1   . ARG A 1 130 ? -16.312 -21.649 -8.371  1.00 13.54 ? 130  ARG A NH1   1 
ATOM   939  N NH2   . ARG A 1 130 ? -18.012 -20.406 -7.531  1.00 13.13 ? 130  ARG A NH2   1 
ATOM   940  N N     . HIS A 1 131 ? -15.982 -21.861 -1.659  1.00 12.39 ? 131  HIS A N     1 
ATOM   941  C CA    . HIS A 1 131 ? -16.290 -21.432 -0.301  1.00 13.04 ? 131  HIS A CA    1 
ATOM   942  C C     . HIS A 1 131 ? -17.326 -20.318 -0.309  1.00 13.76 ? 131  HIS A C     1 
ATOM   943  O O     . HIS A 1 131 ? -17.798 -19.804 -1.341  1.00 13.13 ? 131  HIS A O     1 
ATOM   944  C CB    . HIS A 1 131 ? -15.005 -21.018 0.422   1.00 13.30 ? 131  HIS A CB    1 
ATOM   945  C CG    . HIS A 1 131 ? -14.535 -19.646 0.039   1.00 14.14 ? 131  HIS A CG    1 
ATOM   946  N ND1   . HIS A 1 131 ? -14.293 -18.628 0.962   1.00 14.34 ? 131  HIS A ND1   1 
ATOM   947  C CD2   . HIS A 1 131 ? -14.244 -19.133 -1.186  1.00 14.66 ? 131  HIS A CD2   1 
ATOM   948  C CE1   . HIS A 1 131 ? -13.915 -17.542 0.293   1.00 14.96 ? 131  HIS A CE1   1 
ATOM   949  N NE2   . HIS A 1 131 ? -13.874 -17.821 -1.002  1.00 13.96 ? 131  HIS A NE2   1 
ATOM   950  N N     . VAL A 1 132 ? -17.717 -19.932 0.907   1.00 13.98 ? 132  VAL A N     1 
ATOM   951  C CA    . VAL A 1 132 ? -18.562 -18.763 1.106   1.00 14.03 ? 132  VAL A CA    1 
ATOM   952  C C     . VAL A 1 132 ? -18.029 -18.066 2.349   1.00 12.55 ? 132  VAL A C     1 
ATOM   953  O O     . VAL A 1 132 ? -17.554 -18.767 3.232   1.00 12.55 ? 132  VAL A O     1 
ATOM   954  C CB    . VAL A 1 132 ? -20.017 -19.260 1.268   1.00 16.06 ? 132  VAL A CB    1 
ATOM   955  C CG1   . VAL A 1 132 ? -20.231 -20.097 2.507   1.00 16.37 ? 132  VAL A CG1   1 
ATOM   956  C CG2   . VAL A 1 132 ? -21.067 -18.174 1.161   1.00 18.54 ? 132  VAL A CG2   1 
ATOM   957  N N     . PRO A 1 133 ? -18.101 -16.723 2.462   1.00 14.24 ? 133  PRO A N     1 
ATOM   958  C CA    . PRO A 1 133 ? -17.705 -16.060 3.707   1.00 12.76 ? 133  PRO A CA    1 
ATOM   959  C C     . PRO A 1 133 ? -18.563 -16.608 4.848   1.00 12.29 ? 133  PRO A C     1 
ATOM   960  O O     . PRO A 1 133 ? -19.777 -16.775 4.705   1.00 13.79 ? 133  PRO A O     1 
ATOM   961  C CB    . PRO A 1 133 ? -17.981 -14.562 3.456   1.00 13.50 ? 133  PRO A CB    1 
ATOM   962  C CG    . PRO A 1 133 ? -19.013 -14.590 2.353   1.00 14.00 ? 133  PRO A CG    1 
ATOM   963  C CD    . PRO A 1 133 ? -18.579 -15.757 1.459   1.00 13.40 ? 133  PRO A CD    1 
ATOM   964  N N     . HIS A 1 134 ? -17.906 -16.913 5.965   1.00 13.30 ? 134  HIS A N     1 
ATOM   965  C CA    . HIS A 1 134 ? -18.577 -17.328 7.188   1.00 12.31 ? 134  HIS A CA    1 
ATOM   966  C C     . HIS A 1 134 ? -17.598 -17.171 8.345   1.00 13.62 ? 134  HIS A C     1 
ATOM   967  O O     . HIS A 1 134 ? -16.454 -16.786 8.135   1.00 13.79 ? 134  HIS A O     1 
ATOM   968  C CB    . HIS A 1 134 ? -19.103 -18.757 7.103   1.00 13.27 ? 134  HIS A CB    1 
ATOM   969  C CG    . HIS A 1 134 ? -18.102 -19.778 6.755   1.00 15.32 ? 134  HIS A CG    1 
ATOM   970  N ND1   . HIS A 1 134 ? -17.054 -20.128 7.577   1.00 15.85 ? 134  HIS A ND1   1 
ATOM   971  C CD2   . HIS A 1 134 ? -18.015 -20.561 5.682   1.00 16.84 ? 134  HIS A CD2   1 
ATOM   972  C CE1   . HIS A 1 134 ? -16.344 -21.064 6.961   1.00 16.17 ? 134  HIS A CE1   1 
ATOM   973  N NE2   . HIS A 1 134 ? -16.901 -21.317 5.811   1.00 14.77 ? 134  HIS A NE2   1 
ATOM   974  N N     . GLY A 1 135 ? -18.058 -17.487 9.559   1.00 14.23 ? 135  GLY A N     1 
ATOM   975  C CA    . GLY A 1 135 ? -17.244 -17.353 10.758  1.00 14.94 ? 135  GLY A CA    1 
ATOM   976  C C     . GLY A 1 135 ? -16.148 -18.407 10.808  1.00 14.77 ? 135  GLY A C     1 
ATOM   977  O O     . GLY A 1 135 ? -16.042 -19.277 9.937   1.00 16.29 ? 135  GLY A O     1 
ATOM   978  N N     . THR A 1 136 ? -15.262 -18.270 11.791  1.00 13.88 ? 136  THR A N     1 
ATOM   979  C CA    . THR A 1 136 ? -14.043 -19.042 11.800  1.00 14.92 ? 136  THR A CA    1 
ATOM   980  C C     . THR A 1 136 ? -14.211 -20.305 12.638  1.00 15.61 ? 136  THR A C     1 
ATOM   981  O O     . THR A 1 136 ? -13.436 -21.226 12.460  1.00 19.60 ? 136  THR A O     1 
ATOM   982  C CB    . THR A 1 136 ? -12.845 -18.235 12.305  1.00 17.60 ? 136  THR A CB    1 
ATOM   983  O OG1   . THR A 1 136 ? -13.247 -17.512 13.454  1.00 22.33 ? 136  THR A OG1   1 
ATOM   984  C CG2   . THR A 1 136 ? -12.441 -17.150 11.338  1.00 18.32 ? 136  THR A CG2   1 
ATOM   985  N N     . THR A 1 137 ? -15.219 -20.410 13.495  1.00 14.71 ? 137  THR A N     1 
ATOM   986  C CA    . THR A 1 137 ? -15.273 -21.543 14.427  1.00 14.97 ? 137  THR A CA    1 
ATOM   987  C C     . THR A 1 137 ? -16.072 -22.701 13.794  1.00 13.45 ? 137  THR A C     1 
ATOM   988  O O     . THR A 1 137 ? -17.266 -22.574 13.477  1.00 14.02 ? 137  THR A O     1 
ATOM   989  C CB    . THR A 1 137 ? -15.819 -21.070 15.786  1.00 19.19 ? 137  THR A CB    1 
ATOM   990  O OG1   . THR A 1 137 ? -14.797 -20.292 16.442  1.00 21.00 ? 137  THR A OG1   1 
ATOM   991  C CG2   . THR A 1 137 ? -16.144 -22.258 16.687  1.00 17.42 ? 137  THR A CG2   1 
ATOM   992  N N     . PHE A 1 138 ? -15.424 -23.865 13.679  1.00 13.28 ? 138  PHE A N     1 
ATOM   993  C CA    . PHE A 1 138 ? -15.962 -25.024 12.963  1.00 13.68 ? 138  PHE A CA    1 
ATOM   994  C C     . PHE A 1 138 ? -17.184 -25.639 13.653  1.00 12.72 ? 138  PHE A C     1 
ATOM   995  O O     . PHE A 1 138 ? -17.951 -26.339 12.990  1.00 12.90 ? 138  PHE A O     1 
ATOM   996  C CB    . PHE A 1 138 ? -14.909 -26.102 12.740  1.00 13.05 ? 138  PHE A CB    1 
ATOM   997  C CG    . PHE A 1 138 ? -14.046 -25.928 11.498  1.00 14.53 ? 138  PHE A CG    1 
ATOM   998  C CD1   . PHE A 1 138 ? -14.105 -24.779 10.699  1.00 15.05 ? 138  PHE A CD1   1 
ATOM   999  C CD2   . PHE A 1 138 ? -13.229 -26.973 11.084  1.00 15.26 ? 138  PHE A CD2   1 
ATOM   1000 C CE1   . PHE A 1 138 ? -13.371 -24.684 9.517   1.00 15.96 ? 138  PHE A CE1   1 
ATOM   1001 C CE2   . PHE A 1 138 ? -12.464 -26.856 9.929   1.00 14.31 ? 138  PHE A CE2   1 
ATOM   1002 C CZ    . PHE A 1 138 ? -12.572 -25.734 9.128   1.00 14.90 ? 138  PHE A CZ    1 
ATOM   1003 N N     . THR A 1 139 ? -17.413 -25.380 14.952  1.00 12.61 ? 139  THR A N     1 
ATOM   1004 C CA    . THR A 1 139 ? -18.533 -26.009 15.650  1.00 11.91 ? 139  THR A CA    1 
ATOM   1005 C C     . THR A 1 139 ? -19.795 -25.137 15.588  1.00 11.95 ? 139  THR A C     1 
ATOM   1006 O O     . THR A 1 139 ? -20.850 -25.552 16.044  1.00 13.87 ? 139  THR A O     1 
ATOM   1007 C CB    . THR A 1 139 ? -18.185 -26.273 17.128  1.00 13.65 ? 139  THR A CB    1 
ATOM   1008 O OG1   . THR A 1 139 ? -17.751 -25.048 17.726  1.00 11.46 ? 139  THR A OG1   1 
ATOM   1009 C CG2   . THR A 1 139 ? -17.132 -27.358 17.252  1.00 13.57 ? 139  THR A CG2   1 
ATOM   1010 N N     . VAL A 1 140 ? -19.736 -23.960 14.956  1.00 11.47 ? 140  VAL A N     1 
ATOM   1011 C CA    . VAL A 1 140 ? -20.923 -23.145 14.783  1.00 10.63 ? 140  VAL A CA    1 
ATOM   1012 C C     . VAL A 1 140 ? -21.844 -23.812 13.758  1.00 11.29 ? 140  VAL A C     1 
ATOM   1013 O O     . VAL A 1 140 ? -21.387 -24.402 12.795  1.00 11.49 ? 140  VAL A O     1 
ATOM   1014 C CB    . VAL A 1 140 ? -20.538 -21.712 14.356  1.00 11.97 ? 140  VAL A CB    1 
ATOM   1015 C CG1   . VAL A 1 140 ? -21.714 -20.958 13.748  1.00 11.92 ? 140  VAL A CG1   1 
ATOM   1016 C CG2   . VAL A 1 140 ? -19.928 -20.940 15.502  1.00 13.43 ? 140  VAL A CG2   1 
ATOM   1017 N N     . GLY A 1 141 ? -23.146 -23.773 14.016  1.00 10.86 ? 141  GLY A N     1 
ATOM   1018 C CA    . GLY A 1 141 ? -24.122 -24.402 13.125  1.00 10.64 ? 141  GLY A CA    1 
ATOM   1019 C C     . GLY A 1 141 ? -24.597 -23.414 12.056  1.00 10.67 ? 141  GLY A C     1 
ATOM   1020 O O     . GLY A 1 141 ? -24.766 -22.207 12.295  1.00 12.22 ? 141  GLY A O     1 
ATOM   1021 N N     . LEU A 1 142 ? -24.858 -23.945 10.866  1.00 10.93 ? 142  LEU A N     1 
ATOM   1022 C CA    . LEU A 1 142 ? -25.256 -23.085 9.761   1.00 11.17 ? 142  LEU A CA    1 
ATOM   1023 C C     . LEU A 1 142 ? -26.609 -22.445 10.065  1.00 10.78 ? 142  LEU A C     1 
ATOM   1024 O O     . LEU A 1 142 ? -26.847 -21.259 9.765   1.00 12.00 ? 142  LEU A O     1 
ATOM   1025 C CB    . LEU A 1 142 ? -25.329 -23.980 8.520   1.00 11.24 ? 142  LEU A CB    1 
ATOM   1026 C CG    . LEU A 1 142 ? -25.856 -23.277 7.277   1.00 11.72 ? 142  LEU A CG    1 
ATOM   1027 C CD1   . LEU A 1 142 ? -24.875 -22.193 6.887   1.00 12.82 ? 142  LEU A CD1   1 
ATOM   1028 C CD2   . LEU A 1 142 ? -26.051 -24.282 6.149   1.00 11.55 ? 142  LEU A CD2   1 
ATOM   1029 N N     . GLY A 1 143 ? -27.501 -23.234 10.667  1.00 11.77 ? 143  GLY A N     1 
ATOM   1030 C CA    . GLY A 1 143 ? -28.857 -22.777 10.929  1.00 11.22 ? 143  GLY A CA    1 
ATOM   1031 C C     . GLY A 1 143 ? -28.896 -21.434 11.659  1.00 11.05 ? 143  GLY A C     1 
ATOM   1032 O O     . GLY A 1 143 ? -29.689 -20.554 11.318  1.00 11.92 ? 143  GLY A O     1 
ATOM   1033 N N     . GLY A 1 144 ? -28.123 -21.315 12.738  1.00 10.09 ? 144  GLY A N     1 
ATOM   1034 C CA    . GLY A 1 144 ? -28.157 -20.087 13.515  1.00 10.80 ? 144  GLY A CA    1 
ATOM   1035 C C     . GLY A 1 144 ? -27.211 -19.032 12.965  1.00 11.03 ? 144  GLY A C     1 
ATOM   1036 O O     . GLY A 1 144 ? -27.261 -17.916 13.387  1.00 13.35 ? 144  GLY A O     1 
ATOM   1037 N N     . HIS A 1 145 ? -26.300 -19.417 12.079  1.00 11.16 ? 145  HIS A N     1 
ATOM   1038 C CA    . HIS A 1 145 ? -25.231 -18.548 11.625  1.00 11.68 ? 145  HIS A CA    1 
ATOM   1039 C C     . HIS A 1 145 ? -25.651 -17.779 10.376  1.00 12.04 ? 145  HIS A C     1 
ATOM   1040 O O     . HIS A 1 145 ? -25.529 -16.549 10.293  1.00 11.47 ? 145  HIS A O     1 
ATOM   1041 C CB    . HIS A 1 145 ? -23.984 -19.387 11.392  1.00 11.58 ? 145  HIS A CB    1 
ATOM   1042 C CG    . HIS A 1 145 ? -22.726 -18.670 11.084  1.00 12.09 ? 145  HIS A CG    1 
ATOM   1043 N ND1   . HIS A 1 145 ? -22.143 -17.806 11.986  1.00 12.60 ? 145  HIS A ND1   1 
ATOM   1044 C CD2   . HIS A 1 145 ? -21.921 -18.678 10.004  1.00 12.39 ? 145  HIS A CD2   1 
ATOM   1045 C CE1   . HIS A 1 145 ? -20.991 -17.355 11.468  1.00 14.02 ? 145  HIS A CE1   1 
ATOM   1046 N NE2   . HIS A 1 145 ? -20.860 -17.843 10.249  1.00 13.05 ? 145  HIS A NE2   1 
ATOM   1047 N N     . ALA A 1 146 ? -26.134 -18.513 9.379   1.00 12.43 ? 146  ALA A N     1 
ATOM   1048 C CA    . ALA A 1 146 ? -26.629 -17.878 8.171   1.00 13.02 ? 146  ALA A CA    1 
ATOM   1049 C C     . ALA A 1 146 ? -27.837 -16.984 8.463   1.00 13.48 ? 146  ALA A C     1 
ATOM   1050 O O     . ALA A 1 146 ? -28.193 -16.158 7.631   1.00 14.91 ? 146  ALA A O     1 
ATOM   1051 C CB    . ALA A 1 146 ? -26.952 -18.938 7.154   1.00 12.46 ? 146  ALA A CB    1 
ATOM   1052 N N     . THR A 1 147 ? -28.507 -17.162 9.619   1.00 11.60 ? 147  THR A N     1 
ATOM   1053 C CA    . THR A 1 147 ? -29.711 -16.412 9.919   1.00 11.86 ? 147  THR A CA    1 
ATOM   1054 C C     . THR A 1 147 ? -29.447 -15.211 10.824  1.00 11.43 ? 147  THR A C     1 
ATOM   1055 O O     . THR A 1 147 ? -30.414 -14.540 11.169  1.00 11.49 ? 147  THR A O     1 
ATOM   1056 C CB    . THR A 1 147 ? -30.773 -17.331 10.517  1.00 12.08 ? 147  THR A CB    1 
ATOM   1057 O OG1   . THR A 1 147 ? -30.251 -18.002 11.668  1.00 11.92 ? 147  THR A OG1   1 
ATOM   1058 C CG2   . THR A 1 147 ? -31.224 -18.386 9.532   1.00 11.46 ? 147  THR A CG2   1 
ATOM   1059 N N     . VAL A 1 148 ? -28.190 -14.970 11.225  1.00 11.18 ? 148  VAL A N     1 
ATOM   1060 C CA    . VAL A 1 148 ? -27.836 -13.772 11.976  1.00 11.18 ? 148  VAL A CA    1 
ATOM   1061 C C     . VAL A 1 148 ? -26.931 -12.845 11.181  1.00 12.50 ? 148  VAL A C     1 
ATOM   1062 O O     . VAL A 1 148 ? -26.902 -11.643 11.437  1.00 13.02 ? 148  VAL A O     1 
ATOM   1063 C CB    . VAL A 1 148 ? -27.208 -14.088 13.346  1.00 11.67 ? 148  VAL A CB    1 
ATOM   1064 C CG1   . VAL A 1 148 ? -28.223 -14.792 14.252  1.00 11.89 ? 148  VAL A CG1   1 
ATOM   1065 C CG2   . VAL A 1 148 ? -25.897 -14.862 13.236  1.00 13.14 ? 148  VAL A CG2   1 
ATOM   1066 N N     . GLY A 1 149 ? -26.095 -13.408 10.303  1.00 12.46 ? 149  GLY A N     1 
ATOM   1067 C CA    . GLY A 1 149 ? -25.156 -12.589 9.571   1.00 13.19 ? 149  GLY A CA    1 
ATOM   1068 C C     . GLY A 1 149 ? -24.060 -13.454 8.970   1.00 13.32 ? 149  GLY A C     1 
ATOM   1069 O O     . GLY A 1 149 ? -24.168 -13.891 7.815   1.00 13.04 ? 149  GLY A O     1 
ATOM   1070 N N     . GLY A 1 150 ? -23.054 -13.747 9.805   1.00 12.22 ? 150  GLY A N     1 
ATOM   1071 C CA    . GLY A 1 150 ? -22.018 -14.688 9.436   1.00 13.44 ? 150  GLY A CA    1 
ATOM   1072 C C     . GLY A 1 150 ? -20.841 -13.920 8.839   1.00 13.58 ? 150  GLY A C     1 
ATOM   1073 O O     . GLY A 1 150 ? -20.700 -13.845 7.617   1.00 14.25 ? 150  GLY A O     1 
ATOM   1074 N N     . ALA A 1 151 ? -19.989 -13.385 9.740   1.00 12.41 ? 151  ALA A N     1 
ATOM   1075 C CA    . ALA A 1 151 ? -18.831 -12.593 9.363   1.00 12.74 ? 151  ALA A CA    1 
ATOM   1076 C C     . ALA A 1 151 ? -17.566 -13.365 9.696   1.00 14.00 ? 151  ALA A C     1 
ATOM   1077 O O     . ALA A 1 151 ? -17.439 -13.953 10.775  1.00 15.63 ? 151  ALA A O     1 
ATOM   1078 C CB    . ALA A 1 151 ? -18.852 -11.267 10.078  1.00 14.32 ? 151  ALA A CB    1 
ATOM   1079 N N     . GLY A 1 152 ? -16.617 -13.383 8.759   1.00 13.89 ? 152  GLY A N     1 
ATOM   1080 C CA    . GLY A 1 152 ? -15.347 -14.049 9.013   1.00 12.90 ? 152  GLY A CA    1 
ATOM   1081 C C     . GLY A 1 152 ? -14.238 -13.490 8.130   1.00 13.42 ? 152  GLY A C     1 
ATOM   1082 O O     . GLY A 1 152 ? -14.348 -12.364 7.641   1.00 13.75 ? 152  GLY A O     1 
ATOM   1083 N N     . ALA A 1 153 ? -13.264 -14.340 7.869   1.00 14.06 ? 153  ALA A N     1 
ATOM   1084 C CA    . ALA A 1 153 ? -11.998 -13.958 7.253   1.00 13.97 ? 153  ALA A CA    1 
ATOM   1085 C C     . ALA A 1 153 ? -12.255 -13.361 5.874   1.00 15.24 ? 153  ALA A C     1 
ATOM   1086 O O     . ALA A 1 153 ? -11.642 -12.361 5.523   1.00 14.61 ? 153  ALA A O     1 
ATOM   1087 C CB    . ALA A 1 153 ? -11.107 -15.175 7.198   1.00 14.20 ? 153  ALA A CB    1 
ATOM   1088 N N     . ALA A 1 154 ? -13.237 -13.903 5.129   1.00 14.26 ? 154  ALA A N     1 
ATOM   1089 C CA    . ALA A 1 154 ? -13.505 -13.457 3.770   1.00 15.01 ? 154  ALA A CA    1 
ATOM   1090 C C     . ALA A 1 154 ? -14.597 -12.403 3.658   1.00 14.97 ? 154  ALA A C     1 
ATOM   1091 O O     . ALA A 1 154 ? -14.993 -12.050 2.548   1.00 15.00 ? 154  ALA A O     1 
ATOM   1092 C CB    . ALA A 1 154 ? -13.805 -14.647 2.858   1.00 13.76 ? 154  ALA A CB    1 
ATOM   1093 N N     . SER A 1 155 ? -15.046 -11.825 4.781   1.00 14.10 ? 155  SER A N     1 
ATOM   1094 C CA    . SER A 1 155 ? -16.182 -10.904 4.742   1.00 15.04 ? 155  SER A CA    1 
ATOM   1095 C C     . SER A 1 155 ? -15.839 -9.535  4.142   1.00 13.62 ? 155  SER A C     1 
ATOM   1096 O O     . SER A 1 155 ? -16.668 -9.008  3.411   1.00 12.92 ? 155  SER A O     1 
ATOM   1097 C CB    . SER A 1 155 ? -16.831 -10.769 6.088   1.00 15.73 ? 155  SER A CB    1 
ATOM   1098 O OG    . SER A 1 155 ? -17.562 -11.969 6.389   1.00 15.93 ? 155  SER A OG    1 
ATOM   1099 N N     . ARG A 1 156 ? -14.687 -8.932  4.466   1.00 13.65 ? 156  ARG A N     1 
ATOM   1100 C CA    . ARG A 1 156 ? -14.323 -7.705  3.775   1.00 14.49 ? 156  ARG A CA    1 
ATOM   1101 C C     . ARG A 1 156 ? -14.231 -7.933  2.257   1.00 13.96 ? 156  ARG A C     1 
ATOM   1102 O O     . ARG A 1 156 ? -14.645 -7.057  1.462   1.00 14.41 ? 156  ARG A O     1 
ATOM   1103 C CB    . ARG A 1 156 ? -13.062 -7.066  4.368   1.00 15.52 ? 156  ARG A CB    1 
ATOM   1104 C CG    . ARG A 1 156 ? -13.437 -6.437  5.709   1.00 15.45 ? 156  ARG A CG    1 
ATOM   1105 C CD    . ARG A 1 156 ? -12.249 -5.921  6.445   1.00 16.05 ? 156  ARG A CD    1 
ATOM   1106 N NE    . ARG A 1 156 ? -11.314 -5.167  5.602   1.00 18.68 ? 156  ARG A NE    1 
ATOM   1107 C CZ    . ARG A 1 156 ? -11.409 -3.902  5.358   1.00 18.55 ? 156  ARG A CZ    1 
ATOM   1108 N NH1   . ARG A 1 156 ? -12.424 -3.222  5.834   1.00 22.33 ? 156  ARG A NH1   1 
ATOM   1109 N NH2   . ARG A 1 156 ? -10.487 -3.314  4.650   1.00 20.09 ? 156  ARG A NH2   1 
ATOM   1110 N N     . MET A 1 157 ? -13.840 -9.156  1.858   1.00 14.64 ? 157  MET A N     1 
ATOM   1111 C CA    . MET A 1 157 ? -13.677 -9.474  0.450   1.00 14.99 ? 157  MET A CA    1 
ATOM   1112 C C     . MET A 1 157 ? -15.042 -9.697  -0.209  1.00 15.46 ? 157  MET A C     1 
ATOM   1113 O O     . MET A 1 157 ? -15.250 -9.260  -1.356  1.00 16.80 ? 157  MET A O     1 
ATOM   1114 C CB    . MET A 1 157 ? -12.794 -10.722 0.259   1.00 16.35 ? 157  MET A CB    1 
ATOM   1115 C CG    . MET A 1 157 ? -12.567 -11.138 -1.198  1.00 19.67 ? 157  MET A CG    1 
ATOM   1116 S SD    . MET A 1 157 ? -10.961 -11.963 -1.336  1.00 22.75 ? 157  MET A SD    1 
ATOM   1117 C CE    . MET A 1 157 ? -10.848 -12.468 -3.036  1.00 25.43 ? 157  MET A CE    1 
ATOM   1118 N N     . HIS A 1 158 ? -15.966 -10.405 0.482   1.00 13.68 ? 158  HIS A N     1 
ATOM   1119 C CA    . HIS A 1 158 ? -17.159 -10.941 -0.180  1.00 14.05 ? 158  HIS A CA    1 
ATOM   1120 C C     . HIS A 1 158 ? -18.484 -10.593 0.521   1.00 15.45 ? 158  HIS A C     1 
ATOM   1121 O O     . HIS A 1 158 ? -19.532 -10.760 -0.074  1.00 16.58 ? 158  HIS A O     1 
ATOM   1122 C CB    . HIS A 1 158 ? -17.055 -12.467 -0.294  1.00 13.76 ? 158  HIS A CB    1 
ATOM   1123 C CG    . HIS A 1 158 ? -16.107 -12.930 -1.330  1.00 15.14 ? 158  HIS A CG    1 
ATOM   1124 N ND1   . HIS A 1 158 ? -16.105 -12.417 -2.613  1.00 16.00 ? 158  HIS A ND1   1 
ATOM   1125 C CD2   . HIS A 1 158 ? -15.141 -13.857 -1.286  1.00 16.66 ? 158  HIS A CD2   1 
ATOM   1126 C CE1   . HIS A 1 158 ? -15.159 -13.039 -3.315  1.00 16.09 ? 158  HIS A CE1   1 
ATOM   1127 N NE2   . HIS A 1 158 ? -14.557 -13.917 -2.538  1.00 17.51 ? 158  HIS A NE2   1 
ATOM   1128 N N     . GLY A 1 159 ? -18.473 -10.188 1.798   1.00 14.85 ? 159  GLY A N     1 
ATOM   1129 C CA    . GLY A 1 159 ? -19.701 -9.867  2.523   1.00 13.18 ? 159  GLY A CA    1 
ATOM   1130 C C     . GLY A 1 159 ? -20.055 -10.911 3.583   1.00 13.03 ? 159  GLY A C     1 
ATOM   1131 O O     . GLY A 1 159 ? -19.203 -11.681 4.021   1.00 13.38 ? 159  GLY A O     1 
ATOM   1132 N N     . LEU A 1 160 ? -21.301 -10.870 4.054   1.00 12.41 ? 160  LEU A N     1 
ATOM   1133 C CA    . LEU A 1 160 ? -21.752 -11.824 5.045   1.00 12.77 ? 160  LEU A CA    1 
ATOM   1134 C C     . LEU A 1 160 ? -22.200 -13.120 4.385   1.00 12.66 ? 160  LEU A C     1 
ATOM   1135 O O     . LEU A 1 160 ? -22.662 -13.120 3.250   1.00 12.41 ? 160  LEU A O     1 
ATOM   1136 C CB    . LEU A 1 160 ? -22.887 -11.211 5.854   1.00 13.24 ? 160  LEU A CB    1 
ATOM   1137 C CG    . LEU A 1 160 ? -22.602 -9.867  6.524   1.00 12.38 ? 160  LEU A CG    1 
ATOM   1138 C CD1   . LEU A 1 160 ? -23.856 -9.357  7.205   1.00 12.35 ? 160  LEU A CD1   1 
ATOM   1139 C CD2   . LEU A 1 160 ? -21.433 -9.989  7.496   1.00 14.08 ? 160  LEU A CD2   1 
ATOM   1140 N N     . LEU A 1 161 ? -22.226 -14.190 5.183   1.00 12.38 ? 161  LEU A N     1 
ATOM   1141 C CA    . LEU A 1 161 ? -22.774 -15.446 4.719   1.00 11.91 ? 161  LEU A CA    1 
ATOM   1142 C C     . LEU A 1 161 ? -24.178 -15.222 4.170   1.00 11.87 ? 161  LEU A C     1 
ATOM   1143 O O     . LEU A 1 161 ? -24.578 -15.790 3.132   1.00 12.31 ? 161  LEU A O     1 
ATOM   1144 C CB    . LEU A 1 161 ? -22.795 -16.457 5.860   1.00 11.66 ? 161  LEU A CB    1 
ATOM   1145 C CG    . LEU A 1 161 ? -23.486 -17.767 5.542   1.00 11.81 ? 161  LEU A CG    1 
ATOM   1146 C CD1   . LEU A 1 161 ? -22.954 -18.412 4.269   1.00 11.67 ? 161  LEU A CD1   1 
ATOM   1147 C CD2   . LEU A 1 161 ? -23.331 -18.729 6.719   1.00 12.37 ? 161  LEU A CD2   1 
ATOM   1148 N N     . LEU A 1 162 ? -24.961 -14.417 4.880   1.00 12.17 ? 162  LEU A N     1 
ATOM   1149 C CA    . LEU A 1 162 ? -26.345 -14.276 4.444   1.00 12.54 ? 162  LEU A CA    1 
ATOM   1150 C C     . LEU A 1 162 ? -26.489 -13.532 3.109   1.00 12.79 ? 162  LEU A C     1 
ATOM   1151 O O     . LEU A 1 162 ? -27.533 -13.663 2.457   1.00 13.15 ? 162  LEU A O     1 
ATOM   1152 C CB    . LEU A 1 162 ? -27.269 -13.735 5.523   1.00 12.71 ? 162  LEU A CB    1 
ATOM   1153 C CG    . LEU A 1 162 ? -26.995 -12.349 6.094   1.00 13.64 ? 162  LEU A CG    1 
ATOM   1154 C CD1   . LEU A 1 162 ? -27.304 -11.280 5.102   1.00 15.14 ? 162  LEU A CD1   1 
ATOM   1155 C CD2   . LEU A 1 162 ? -27.845 -12.175 7.355   1.00 12.78 ? 162  LEU A CD2   1 
ATOM   1156 N N     . ASP A 1 163 ? -25.450 -12.815 2.663   1.00 12.81 ? 163  ASP A N     1 
ATOM   1157 C CA    . ASP A 1 163 ? -25.411 -12.200 1.340   1.00 13.57 ? 163  ASP A CA    1 
ATOM   1158 C C     . ASP A 1 163 ? -25.320 -13.250 0.225   1.00 14.42 ? 163  ASP A C     1 
ATOM   1159 O O     . ASP A 1 163 ? -25.572 -12.929 -0.939  1.00 16.94 ? 163  ASP A O     1 
ATOM   1160 C CB    . ASP A 1 163 ? -24.272 -11.194 1.253   1.00 14.30 ? 163  ASP A CB    1 
ATOM   1161 C CG    . ASP A 1 163 ? -24.495 -9.998  2.156   1.00 14.21 ? 163  ASP A CG    1 
ATOM   1162 O OD1   . ASP A 1 163 ? -25.680 -9.656  2.305   1.00 14.46 ? 163  ASP A OD1   1 
ATOM   1163 O OD2   . ASP A 1 163 ? -23.504 -9.457  2.727   1.00 14.76 ? 163  ASP A OD2   1 
ATOM   1164 N N     . TYR A 1 164 ? -25.001 -14.494 0.577   1.00 11.61 ? 164  TYR A N     1 
ATOM   1165 C CA    . TYR A 1 164 ? -24.912 -15.577 -0.391  1.00 12.33 ? 164  TYR A CA    1 
ATOM   1166 C C     . TYR A 1 164 ? -26.105 -16.523 -0.308  1.00 12.35 ? 164  TYR A C     1 
ATOM   1167 O O     . TYR A 1 164 ? -26.200 -17.473 -1.095  1.00 12.84 ? 164  TYR A O     1 
ATOM   1168 C CB    . TYR A 1 164 ? -23.579 -16.304 -0.189  1.00 13.19 ? 164  TYR A CB    1 
ATOM   1169 C CG    . TYR A 1 164 ? -22.428 -15.539 -0.808  1.00 13.64 ? 164  TYR A CG    1 
ATOM   1170 C CD1   . TYR A 1 164 ? -21.888 -14.427 -0.166  1.00 12.93 ? 164  TYR A CD1   1 
ATOM   1171 C CD2   . TYR A 1 164 ? -21.910 -15.900 -2.043  1.00 13.43 ? 164  TYR A CD2   1 
ATOM   1172 C CE1   . TYR A 1 164 ? -20.907 -13.672 -0.767  1.00 12.38 ? 164  TYR A CE1   1 
ATOM   1173 C CE2   . TYR A 1 164 ? -20.889 -15.174 -2.636  1.00 12.83 ? 164  TYR A CE2   1 
ATOM   1174 C CZ    . TYR A 1 164 ? -20.364 -14.075 -1.975  1.00 12.15 ? 164  TYR A CZ    1 
ATOM   1175 O OH    . TYR A 1 164 ? -19.366 -13.311 -2.542  1.00 14.90 ? 164  TYR A OH    1 
ATOM   1176 N N     . VAL A 1 165 ? -26.996 -16.302 0.663   1.00 12.97 ? 165  VAL A N     1 
ATOM   1177 C CA    . VAL A 1 165 ? -28.178 -17.137 0.788   1.00 13.63 ? 165  VAL A CA    1 
ATOM   1178 C C     . VAL A 1 165 ? -29.148 -16.681 -0.303  1.00 13.73 ? 165  VAL A C     1 
ATOM   1179 O O     . VAL A 1 165 ? -29.521 -15.515 -0.331  1.00 14.50 ? 165  VAL A O     1 
ATOM   1180 C CB    . VAL A 1 165 ? -28.801 -17.063 2.191   1.00 13.38 ? 165  VAL A CB    1 
ATOM   1181 C CG1   . VAL A 1 165 ? -30.169 -17.732 2.217   1.00 13.74 ? 165  VAL A CG1   1 
ATOM   1182 C CG2   . VAL A 1 165 ? -27.880 -17.603 3.275   1.00 12.89 ? 165  VAL A CG2   1 
ATOM   1183 N N     . GLU A 1 166 ? -29.489 -17.582 -1.228  1.00 13.57 ? 166  GLU A N     1 
ATOM   1184 C CA    . GLU A 1 166 ? -30.362 -17.255 -2.362  1.00 16.06 ? 166  GLU A CA    1 
ATOM   1185 C C     . GLU A 1 166 ? -31.813 -17.693 -2.143  1.00 15.12 ? 166  GLU A C     1 
ATOM   1186 O O     . GLU A 1 166 ? -32.743 -17.077 -2.656  1.00 15.89 ? 166  GLU A O     1 
ATOM   1187 C CB    . GLU A 1 166 ? -29.779 -18.023 -3.551  1.00 20.92 ? 166  GLU A CB    1 
ATOM   1188 C CG    . GLU A 1 166 ? -30.675 -18.078 -4.779  1.00 28.48 ? 166  GLU A CG    1 
ATOM   1189 C CD    . GLU A 1 166 ? -29.896 -18.866 -5.807  1.00 38.72 ? 166  GLU A CD    1 
ATOM   1190 O OE1   . GLU A 1 166 ? -30.258 -20.037 -6.143  1.00 46.42 ? 166  GLU A OE1   1 
ATOM   1191 O OE2   . GLU A 1 166 ? -28.865 -18.274 -6.178  1.00 38.44 ? 166  GLU A OE2   1 
ATOM   1192 N N     . GLU A 1 167 ? -32.013 -18.761 -1.367  1.00 13.72 ? 167  GLU A N     1 
ATOM   1193 C CA    . GLU A 1 167 ? -33.350 -19.235 -1.077  1.00 13.89 ? 167  GLU A CA    1 
ATOM   1194 C C     . GLU A 1 167 ? -33.304 -20.059 0.210   1.00 13.61 ? 167  GLU A C     1 
ATOM   1195 O O     . GLU A 1 167 ? -32.284 -20.642 0.566   1.00 12.87 ? 167  GLU A O     1 
ATOM   1196 C CB    . GLU A 1 167 ? -33.828 -20.066 -2.267  1.00 16.17 ? 167  GLU A CB    1 
ATOM   1197 C CG    . GLU A 1 167 ? -35.323 -20.353 -2.235  1.00 17.99 ? 167  GLU A CG    1 
ATOM   1198 C CD    . GLU A 1 167 ? -35.875 -21.245 -3.351  1.00 23.13 ? 167  GLU A CD    1 
ATOM   1199 O OE1   . GLU A 1 167 ? -35.202 -22.202 -3.779  1.00 30.60 ? 167  GLU A OE1   1 
ATOM   1200 O OE2   . GLU A 1 167 ? -37.077 -21.115 -3.629  1.00 25.65 ? 167  GLU A OE2   1 
ATOM   1201 N N     . VAL A 1 168 ? -34.438 -20.081 0.900   1.00 12.45 ? 168  VAL A N     1 
ATOM   1202 C CA    . VAL A 1 168 ? -34.621 -20.945 2.059   1.00 13.05 ? 168  VAL A CA    1 
ATOM   1203 C C     . VAL A 1 168 ? -35.961 -21.652 1.986   1.00 12.61 ? 168  VAL A C     1 
ATOM   1204 O O     . VAL A 1 168 ? -36.891 -21.203 1.341   1.00 11.72 ? 168  VAL A O     1 
ATOM   1205 C CB    . VAL A 1 168 ? -34.516 -20.156 3.367   1.00 13.25 ? 168  VAL A CB    1 
ATOM   1206 C CG1   . VAL A 1 168 ? -33.076 -19.751 3.644   1.00 13.34 ? 168  VAL A CG1   1 
ATOM   1207 C CG2   . VAL A 1 168 ? -35.461 -18.974 3.347   1.00 13.90 ? 168  VAL A CG2   1 
ATOM   1208 N N     . GLU A 1 169 ? -36.038 -22.774 2.690   1.00 12.15 ? 169  GLU A N     1 
ATOM   1209 C CA    . GLU A 1 169 ? -37.292 -23.404 3.072   1.00 11.15 ? 169  GLU A CA    1 
ATOM   1210 C C     . GLU A 1 169 ? -37.491 -23.129 4.559   1.00 11.35 ? 169  GLU A C     1 
ATOM   1211 O O     . GLU A 1 169 ? -36.541 -23.295 5.350   1.00 11.61 ? 169  GLU A O     1 
ATOM   1212 C CB    . GLU A 1 169 ? -37.172 -24.903 2.833   1.00 11.72 ? 169  GLU A CB    1 
ATOM   1213 C CG    . GLU A 1 169 ? -38.461 -25.660 3.101   1.00 12.08 ? 169  GLU A CG    1 
ATOM   1214 C CD    . GLU A 1 169 ? -38.387 -27.165 2.941   1.00 14.26 ? 169  GLU A CD    1 
ATOM   1215 O OE1   . GLU A 1 169 ? -37.522 -27.767 3.619   1.00 14.61 ? 169  GLU A OE1   1 
ATOM   1216 O OE2   . GLU A 1 169 ? -39.225 -27.710 2.187   1.00 15.64 ? 169  GLU A OE2   1 
ATOM   1217 N N     . VAL A 1 170 ? -38.730 -22.798 4.928   1.00 11.81 ? 170  VAL A N     1 
ATOM   1218 C CA    . VAL A 1 170 ? -39.021 -22.328 6.278   1.00 11.95 ? 170  VAL A CA    1 
ATOM   1219 C C     . VAL A 1 170 ? -40.288 -23.021 6.760   1.00 12.31 ? 170  VAL A C     1 
ATOM   1220 O O     . VAL A 1 170 ? -41.287 -23.077 6.025   1.00 11.89 ? 170  VAL A O     1 
ATOM   1221 C CB    . VAL A 1 170 ? -39.219 -20.810 6.344   1.00 14.64 ? 170  VAL A CB    1 
ATOM   1222 C CG1   . VAL A 1 170 ? -39.352 -20.345 7.790   1.00 17.75 ? 170  VAL A CG1   1 
ATOM   1223 C CG2   . VAL A 1 170 ? -38.125 -20.019 5.631   1.00 15.57 ? 170  VAL A CG2   1 
ATOM   1224 N N     . VAL A 1 171 ? -40.221 -23.554 7.975   1.00 11.16 ? 171  VAL A N     1 
ATOM   1225 C CA    . VAL A 1 171 ? -41.406 -24.016 8.677   1.00 11.12 ? 171  VAL A CA    1 
ATOM   1226 C C     . VAL A 1 171 ? -41.946 -22.868 9.519   1.00 11.74 ? 171  VAL A C     1 
ATOM   1227 O O     . VAL A 1 171 ? -41.241 -22.288 10.361  1.00 10.59 ? 171  VAL A O     1 
ATOM   1228 C CB    . VAL A 1 171 ? -41.181 -25.285 9.506   1.00 12.58 ? 171  VAL A CB    1 
ATOM   1229 C CG1   . VAL A 1 171 ? -42.397 -25.669 10.328  1.00 13.07 ? 171  VAL A CG1   1 
ATOM   1230 C CG2   . VAL A 1 171 ? -40.703 -26.451 8.652   1.00 13.12 ? 171  VAL A CG2   1 
ATOM   1231 N N     . LEU A 1 172 ? -43.222 -22.558 9.279   1.00 12.08 ? 172  LEU A N     1 
ATOM   1232 C CA    . LEU A 1 172 ? -43.888 -21.464 9.980   1.00 12.51 ? 172  LEU A CA    1 
ATOM   1233 C C     . LEU A 1 172 ? -44.615 -21.977 11.220  1.00 12.21 ? 172  LEU A C     1 
ATOM   1234 O O     . LEU A 1 172 ? -44.763 -23.181 11.451  1.00 11.97 ? 172  LEU A O     1 
ATOM   1235 C CB    . LEU A 1 172 ? -44.846 -20.765 9.018   1.00 13.07 ? 172  LEU A CB    1 
ATOM   1236 C CG    . LEU A 1 172 ? -44.207 -20.209 7.739   1.00 14.74 ? 172  LEU A CG    1 
ATOM   1237 C CD1   . LEU A 1 172 ? -45.237 -19.565 6.819   1.00 16.53 ? 172  LEU A CD1   1 
ATOM   1238 C CD2   . LEU A 1 172 ? -43.108 -19.225 8.056   1.00 15.24 ? 172  LEU A CD2   1 
ATOM   1239 N N     . ALA A 1 173 ? -45.072 -21.024 12.045  1.00 12.25 ? 173  ALA A N     1 
ATOM   1240 C CA    . ALA A 1 173 ? -45.699 -21.329 13.309  1.00 11.93 ? 173  ALA A CA    1 
ATOM   1241 C C     . ALA A 1 173 ? -46.984 -22.161 13.171  1.00 12.87 ? 173  ALA A C     1 
ATOM   1242 O O     . ALA A 1 173 ? -47.375 -22.853 14.101  1.00 13.47 ? 173  ALA A O     1 
ATOM   1243 C CB    . ALA A 1 173 ? -45.936 -20.011 14.012  1.00 12.68 ? 173  ALA A CB    1 
ATOM   1244 N N     . ASN A 1 174 ? -47.659 -22.105 12.006  1.00 11.83 ? 174  ASN A N     1 
ATOM   1245 C CA    . ASN A 1 174 ? -48.862 -22.888 11.777  1.00 13.18 ? 174  ASN A CA    1 
ATOM   1246 C C     . ASN A 1 174 ? -48.565 -24.189 11.045  1.00 14.19 ? 174  ASN A C     1 
ATOM   1247 O O     . ASN A 1 174 ? -49.483 -24.866 10.585  1.00 14.02 ? 174  ASN A O     1 
ATOM   1248 C CB    . ASN A 1 174 ? -49.906 -22.100 11.005  1.00 14.78 ? 174  ASN A CB    1 
ATOM   1249 C CG    . ASN A 1 174 ? -49.400 -21.621 9.676   1.00 14.22 ? 174  ASN A CG    1 
ATOM   1250 O OD1   . ASN A 1 174 ? -48.318 -22.011 9.208   1.00 11.78 ? 174  ASN A OD1   1 
ATOM   1251 N ND2   . ASN A 1 174 ? -50.186 -20.751 9.070   1.00 15.39 ? 174  ASN A ND2   1 
ATOM   1252 N N     . SER A 1 175 ? -47.276 -24.554 11.017  1.00 13.31 ? 175  SER A N     1 
ATOM   1253 C CA    . SER A 1 175 ? -46.822 -25.784 10.385  1.00 12.79 ? 175  SER A CA    1 
ATOM   1254 C C     . SER A 1 175 ? -46.999 -25.811 8.853   1.00 12.59 ? 175  SER A C     1 
ATOM   1255 O O     . SER A 1 175 ? -46.854 -26.879 8.265   1.00 14.14 ? 175  SER A O     1 
ATOM   1256 C CB    . SER A 1 175 ? -47.399 -27.016 11.037  1.00 14.64 ? 175  SER A CB    1 
ATOM   1257 O OG    . SER A 1 175 ? -46.933 -27.111 12.383  1.00 15.09 ? 175  SER A OG    1 
ATOM   1258 N N     . SER A 1 176 ? -47.188 -24.653 8.218   1.00 12.69 ? 176  SER A N     1 
ATOM   1259 C CA    . SER A 1 176 ? -47.045 -24.488 6.784   1.00 13.09 ? 176  SER A CA    1 
ATOM   1260 C C     . SER A 1 176 ? -45.560 -24.464 6.480   1.00 14.10 ? 176  SER A C     1 
ATOM   1261 O O     . SER A 1 176 ? -44.760 -24.016 7.307   1.00 13.85 ? 176  SER A O     1 
ATOM   1262 C CB    . SER A 1 176 ? -47.688 -23.207 6.258   1.00 13.82 ? 176  SER A CB    1 
ATOM   1263 O OG    . SER A 1 176 ? -49.100 -23.327 6.263   1.00 15.10 ? 176  SER A OG    1 
ATOM   1264 N N     . ILE A 1 177 ? -45.222 -24.994 5.307   1.00 11.95 ? 177  ILE A N     1 
ATOM   1265 C CA    . ILE A 1 177 ? -43.858 -25.045 4.798   1.00 12.79 ? 177  ILE A CA    1 
ATOM   1266 C C     . ILE A 1 177 ? -43.832 -24.136 3.577   1.00 15.01 ? 177  ILE A C     1 
ATOM   1267 O O     . ILE A 1 177 ? -44.650 -24.293 2.664   1.00 16.82 ? 177  ILE A O     1 
ATOM   1268 C CB    . ILE A 1 177 ? -43.412 -26.479 4.440   1.00 12.38 ? 177  ILE A CB    1 
ATOM   1269 C CG1   . ILE A 1 177 ? -43.574 -27.459 5.599   1.00 14.17 ? 177  ILE A CG1   1 
ATOM   1270 C CG2   . ILE A 1 177 ? -41.981 -26.421 3.889   1.00 14.03 ? 177  ILE A CG2   1 
ATOM   1271 C CD1   . ILE A 1 177 ? -43.436 -28.929 5.236   1.00 13.27 ? 177  ILE A CD1   1 
ATOM   1272 N N     . VAL A 1 178 ? -42.941 -23.148 3.583   1.00 13.36 ? 178  VAL A N     1 
ATOM   1273 C CA    . VAL A 1 178 ? -42.853 -22.191 2.499   1.00 13.65 ? 178  VAL A CA    1 
ATOM   1274 C C     . VAL A 1 178 ? -41.398 -22.083 2.051   1.00 14.32 ? 178  VAL A C     1 
ATOM   1275 O O     . VAL A 1 178 ? -40.467 -22.496 2.757   1.00 13.12 ? 178  VAL A O     1 
ATOM   1276 C CB    . VAL A 1 178 ? -43.375 -20.810 2.905   1.00 15.04 ? 178  VAL A CB    1 
ATOM   1277 C CG1   . VAL A 1 178 ? -44.849 -20.845 3.297   1.00 16.78 ? 178  VAL A CG1   1 
ATOM   1278 C CG2   . VAL A 1 178 ? -42.560 -20.243 4.073   1.00 15.49 ? 178  VAL A CG2   1 
ATOM   1279 N N     . ARG A 1 179 ? -41.231 -21.406 0.912   1.00 16.14 ? 179  ARG A N     1 
ATOM   1280 C CA    . ARG A 1 179 ? -39.926 -20.974 0.436   1.00 16.41 ? 179  ARG A CA    1 
ATOM   1281 C C     . ARG A 1 179 ? -39.864 -19.463 0.432   1.00 15.77 ? 179  ARG A C     1 
ATOM   1282 O O     . ARG A 1 179 ? -40.883 -18.758 0.335   1.00 16.94 ? 179  ARG A O     1 
ATOM   1283 C CB    . ARG A 1 179 ? -39.635 -21.546 -0.956  1.00 16.75 ? 179  ARG A CB    1 
ATOM   1284 C CG    . ARG A 1 179 ? -39.757 -23.061 -0.945  1.00 19.67 ? 179  ARG A CG    1 
ATOM   1285 C CD    . ARG A 1 179 ? -39.337 -23.676 -2.268  1.00 22.42 ? 179  ARG A CD    1 
ATOM   1286 N NE    . ARG A 1 179 ? -37.890 -23.560 -2.323  1.00 28.26 ? 179  ARG A NE    1 
ATOM   1287 C CZ    . ARG A 1 179 ? -37.042 -24.357 -1.653  1.00 33.44 ? 179  ARG A CZ    1 
ATOM   1288 N NH1   . ARG A 1 179 ? -35.738 -24.191 -1.816  1.00 34.96 ? 179  ARG A NH1   1 
ATOM   1289 N NH2   . ARG A 1 179 ? -37.496 -25.324 -0.869  1.00 31.17 ? 179  ARG A NH2   1 
ATOM   1290 N N     . ALA A 1 180 ? -38.640 -18.955 0.507   1.00 14.19 ? 180  ALA A N     1 
ATOM   1291 C CA    . ALA A 1 180 ? -38.450 -17.520 0.458   1.00 13.84 ? 180  ALA A CA    1 
ATOM   1292 C C     . ALA A 1 180 ? -37.156 -17.194 -0.270  1.00 14.64 ? 180  ALA A C     1 
ATOM   1293 O O     . ALA A 1 180 ? -36.190 -17.936 -0.188  1.00 15.02 ? 180  ALA A O     1 
ATOM   1294 C CB    . ALA A 1 180 ? -38.509 -16.913 1.839   1.00 14.37 ? 180  ALA A CB    1 
ATOM   1295 N N     . SER A 1 181 ? -37.170 -16.072 -1.007  1.00 14.65 ? 181  SER A N     1 
ATOM   1296 C CA    . SER A 1 181 ? -36.061 -15.619 -1.822  1.00 15.97 ? 181  SER A CA    1 
ATOM   1297 C C     . SER A 1 181 ? -36.322 -14.149 -2.111  1.00 17.54 ? 181  SER A C     1 
ATOM   1298 O O     . SER A 1 181 ? -37.345 -13.634 -1.685  1.00 18.98 ? 181  SER A O     1 
ATOM   1299 C CB    . SER A 1 181 ? -35.939 -16.417 -3.091  1.00 16.82 ? 181  SER A CB    1 
ATOM   1300 O OG    . SER A 1 181 ? -37.107 -16.212 -3.883  1.00 17.85 ? 181  SER A OG    1 
ATOM   1301 N N     . LYS A 1 182 ? -35.448 -13.487 -2.879  1.00 20.31 ? 182  LYS A N     1 
ATOM   1302 C CA    . LYS A 1 182 ? -35.640 -12.065 -3.152  1.00 23.40 ? 182  LYS A CA    1 
ATOM   1303 C C     . LYS A 1 182 ? -36.883 -11.837 -4.026  1.00 23.84 ? 182  LYS A C     1 
ATOM   1304 O O     . LYS A 1 182 ? -37.415 -10.739 -4.028  1.00 25.80 ? 182  LYS A O     1 
ATOM   1305 C CB    . LYS A 1 182 ? -34.395 -11.430 -3.792  1.00 29.37 ? 182  LYS A CB    1 
ATOM   1306 C CG    . LYS A 1 182 ? -33.409 -10.914 -2.728  1.00 39.49 ? 182  LYS A CG    1 
ATOM   1307 C CD    . LYS A 1 182 ? -32.285 -9.972  -3.165  1.00 47.68 ? 182  LYS A CD    1 
ATOM   1308 C CE    . LYS A 1 182 ? -31.247 -10.586 -4.055  1.00 55.79 ? 182  LYS A CE    1 
ATOM   1309 N NZ    . LYS A 1 182 ? -30.592 -11.761 -3.470  1.00 62.01 ? 182  LYS A NZ    1 
ATOM   1310 N N     . SER A 1 183 ? -37.361 -12.882 -4.697  1.00 21.09 ? 183  SER A N     1 
ATOM   1311 C CA    . SER A 1 183 ? -38.456 -12.788 -5.647  1.00 23.28 ? 183  SER A CA    1 
ATOM   1312 C C     . SER A 1 183 ? -39.754 -13.399 -5.126  1.00 23.36 ? 183  SER A C     1 
ATOM   1313 O O     . SER A 1 183 ? -40.766 -13.320 -5.810  1.00 22.99 ? 183  SER A O     1 
ATOM   1314 C CB    . SER A 1 183 ? -38.056 -13.477 -6.964  1.00 25.06 ? 183  SER A CB    1 
ATOM   1315 O OG    . SER A 1 183 ? -37.572 -14.792 -6.690  1.00 28.68 ? 183  SER A OG    1 
ATOM   1316 N N     . HIS A 1 184 ? -39.746 -14.002 -3.929  1.00 19.18 ? 184  HIS A N     1 
ATOM   1317 C CA    . HIS A 1 184 ? -40.876 -14.773 -3.475  1.00 17.14 ? 184  HIS A CA    1 
ATOM   1318 C C     . HIS A 1 184 ? -40.904 -14.760 -1.947  1.00 16.93 ? 184  HIS A C     1 
ATOM   1319 O O     . HIS A 1 184 ? -39.908 -15.136 -1.314  1.00 16.69 ? 184  HIS A O     1 
ATOM   1320 C CB    . HIS A 1 184 ? -40.763 -16.184 -4.057  1.00 19.47 ? 184  HIS A CB    1 
ATOM   1321 C CG    . HIS A 1 184 ? -41.804 -17.128 -3.565  1.00 20.80 ? 184  HIS A CG    1 
ATOM   1322 N ND1   . HIS A 1 184 ? -43.140 -16.984 -3.883  1.00 24.13 ? 184  HIS A ND1   1 
ATOM   1323 C CD2   . HIS A 1 184 ? -41.728 -18.199 -2.757  1.00 24.40 ? 184  HIS A CD2   1 
ATOM   1324 C CE1   . HIS A 1 184 ? -43.843 -17.921 -3.266  1.00 26.96 ? 184  HIS A CE1   1 
ATOM   1325 N NE2   . HIS A 1 184 ? -43.002 -18.695 -2.605  1.00 26.17 ? 184  HIS A NE2   1 
ATOM   1326 N N     . ASN A 1 185 ? -42.027 -14.345 -1.361  1.00 16.69 ? 185  ASN A N     1 
ATOM   1327 C CA    . ASN A 1 185 ? -42.074 -14.149 0.087   1.00 16.26 ? 185  ASN A CA    1 
ATOM   1328 C C     . ASN A 1 185 ? -40.862 -13.311 0.516   1.00 17.71 ? 185  ASN A C     1 
ATOM   1329 O O     . ASN A 1 185 ? -40.145 -13.671 1.463   1.00 15.49 ? 185  ASN A O     1 
ATOM   1330 C CB    . ASN A 1 185 ? -42.136 -15.482 0.831   1.00 17.25 ? 185  ASN A CB    1 
ATOM   1331 C CG    . ASN A 1 185 ? -43.438 -16.220 0.615   1.00 19.47 ? 185  ASN A CG    1 
ATOM   1332 O OD1   . ASN A 1 185 ? -44.512 -15.599 0.530   1.00 21.32 ? 185  ASN A OD1   1 
ATOM   1333 N ND2   . ASN A 1 185 ? -43.372 -17.541 0.549   1.00 20.72 ? 185  ASN A ND2   1 
ATOM   1334 N N     . GLU A 1 186 ? -40.682 -12.160 -0.147  1.00 17.86 ? 186  GLU A N     1 
ATOM   1335 C CA    . GLU A 1 186 ? -39.569 -11.258 0.080   1.00 19.94 ? 186  GLU A CA    1 
ATOM   1336 C C     . GLU A 1 186 ? -39.526 -10.774 1.529   1.00 16.88 ? 186  GLU A C     1 
ATOM   1337 O O     . GLU A 1 186 ? -38.446 -10.586 2.078   1.00 16.10 ? 186  GLU A O     1 
ATOM   1338 C CB    . GLU A 1 186 ? -39.744 -10.123 -0.932  1.00 25.21 ? 186  GLU A CB    1 
ATOM   1339 C CG    . GLU A 1 186 ? -38.718 -9.010  -0.840  1.00 38.62 ? 186  GLU A CG    1 
ATOM   1340 C CD    . GLU A 1 186 ? -38.801 -8.081  -2.050  1.00 51.95 ? 186  GLU A CD    1 
ATOM   1341 O OE1   . GLU A 1 186 ? -37.755 -7.929  -2.727  1.00 63.35 ? 186  GLU A OE1   1 
ATOM   1342 O OE2   . GLU A 1 186 ? -39.905 -7.550  -2.334  1.00 55.59 ? 186  GLU A OE2   1 
ATOM   1343 N N     . ASP A 1 187 ? -40.686 -10.554 2.161   1.00 16.97 ? 187  ASP A N     1 
ATOM   1344 C CA    . ASP A 1 187 ? -40.720 -10.093 3.545   1.00 15.69 ? 187  ASP A CA    1 
ATOM   1345 C C     . ASP A 1 187 ? -40.143 -11.150 4.493   1.00 14.50 ? 187  ASP A C     1 
ATOM   1346 O O     . ASP A 1 187 ? -39.296 -10.873 5.370   1.00 14.44 ? 187  ASP A O     1 
ATOM   1347 C CB    . ASP A 1 187 ? -42.117 -9.753  4.013   1.00 16.34 ? 187  ASP A CB    1 
ATOM   1348 C CG    . ASP A 1 187 ? -42.688 -8.459  3.449   1.00 23.89 ? 187  ASP A CG    1 
ATOM   1349 O OD1   . ASP A 1 187 ? -41.947 -7.708  2.768   1.00 27.04 ? 187  ASP A OD1   1 
ATOM   1350 O OD2   . ASP A 1 187 ? -43.878 -8.214  3.731   1.00 29.02 ? 187  ASP A OD2   1 
ATOM   1351 N N     . LEU A 1 188 ? -40.580 -12.388 4.314   1.00 14.32 ? 188  LEU A N     1 
ATOM   1352 C CA    . LEU A 1 188 ? -40.038 -13.476 5.125   1.00 14.44 ? 188  LEU A CA    1 
ATOM   1353 C C     . LEU A 1 188 ? -38.539 -13.612 4.870   1.00 14.61 ? 188  LEU A C     1 
ATOM   1354 O O     . LEU A 1 188 ? -37.770 -13.878 5.795   1.00 14.71 ? 188  LEU A O     1 
ATOM   1355 C CB    . LEU A 1 188 ? -40.716 -14.787 4.780   1.00 14.92 ? 188  LEU A CB    1 
ATOM   1356 C CG    . LEU A 1 188 ? -40.274 -16.023 5.569   1.00 15.25 ? 188  LEU A CG    1 
ATOM   1357 C CD1   . LEU A 1 188 ? -40.498 -15.859 7.089   1.00 15.49 ? 188  LEU A CD1   1 
ATOM   1358 C CD2   . LEU A 1 188 ? -41.036 -17.218 5.096   1.00 15.49 ? 188  LEU A CD2   1 
ATOM   1359 N N     . PHE A 1 189 ? -38.137 -13.431 3.605   1.00 14.57 ? 189  PHE A N     1 
ATOM   1360 C CA    . PHE A 1 189 ? -36.733 -13.593 3.258   1.00 14.57 ? 189  PHE A CA    1 
ATOM   1361 C C     . PHE A 1 189 ? -35.888 -12.543 3.973   1.00 14.16 ? 189  PHE A C     1 
ATOM   1362 O O     . PHE A 1 189 ? -34.813 -12.859 4.512   1.00 14.34 ? 189  PHE A O     1 
ATOM   1363 C CB    . PHE A 1 189 ? -36.567 -13.543 1.739   1.00 14.59 ? 189  PHE A CB    1 
ATOM   1364 C CG    . PHE A 1 189 ? -35.207 -14.010 1.246   1.00 14.49 ? 189  PHE A CG    1 
ATOM   1365 C CD1   . PHE A 1 189 ? -34.752 -15.281 1.553   1.00 15.19 ? 189  PHE A CD1   1 
ATOM   1366 C CD2   . PHE A 1 189 ? -34.409 -13.173 0.483   1.00 16.69 ? 189  PHE A CD2   1 
ATOM   1367 C CE1   . PHE A 1 189 ? -33.535 -15.728 1.055   1.00 16.37 ? 189  PHE A CE1   1 
ATOM   1368 C CE2   . PHE A 1 189 ? -33.192 -13.639 -0.014  1.00 16.57 ? 189  PHE A CE2   1 
ATOM   1369 C CZ    . PHE A 1 189 ? -32.762 -14.907 0.298   1.00 16.13 ? 189  PHE A CZ    1 
ATOM   1370 N N     . PHE A 1 190 ? -36.426 -11.327 4.077   1.00 13.57 ? 190  PHE A N     1 
ATOM   1371 C CA    . PHE A 1 190 ? -35.770 -10.242 4.789   1.00 13.85 ? 190  PHE A CA    1 
ATOM   1372 C C     . PHE A 1 190 ? -35.584 -10.623 6.249   1.00 14.44 ? 190  PHE A C     1 
ATOM   1373 O O     . PHE A 1 190 ? -34.521 -10.413 6.820   1.00 14.11 ? 190  PHE A O     1 
ATOM   1374 C CB    . PHE A 1 190 ? -36.611 -8.974  4.624   1.00 14.15 ? 190  PHE A CB    1 
ATOM   1375 C CG    . PHE A 1 190 ? -36.301 -7.873  5.624   1.00 14.23 ? 190  PHE A CG    1 
ATOM   1376 C CD1   . PHE A 1 190 ? -35.284 -6.961  5.394   1.00 14.19 ? 190  PHE A CD1   1 
ATOM   1377 C CD2   . PHE A 1 190 ? -37.043 -7.760  6.792   1.00 14.97 ? 190  PHE A CD2   1 
ATOM   1378 C CE1   . PHE A 1 190 ? -34.999 -5.971  6.325   1.00 14.34 ? 190  PHE A CE1   1 
ATOM   1379 C CE2   . PHE A 1 190 ? -36.759 -6.763  7.708   1.00 14.78 ? 190  PHE A CE2   1 
ATOM   1380 C CZ    . PHE A 1 190 ? -35.740 -5.877  7.472   1.00 15.06 ? 190  PHE A CZ    1 
ATOM   1381 N N     . ALA A 1 191 ? -36.625 -11.176 6.853   1.00 13.97 ? 191  ALA A N     1 
ATOM   1382 C CA    . ALA A 1 191 ? -36.569 -11.502 8.265   1.00 13.53 ? 191  ALA A CA    1 
ATOM   1383 C C     . ALA A 1 191 ? -35.672 -12.708 8.553   1.00 13.56 ? 191  ALA A C     1 
ATOM   1384 O O     . ALA A 1 191 ? -34.943 -12.747 9.543   1.00 12.79 ? 191  ALA A O     1 
ATOM   1385 C CB    . ALA A 1 191 ? -37.981 -11.763 8.751   1.00 14.18 ? 191  ALA A CB    1 
ATOM   1386 N N     . VAL A 1 192 ? -35.681 -13.680 7.647   1.00 12.96 ? 192  VAL A N     1 
ATOM   1387 C CA    . VAL A 1 192 ? -34.826 -14.847 7.798   1.00 13.57 ? 192  VAL A CA    1 
ATOM   1388 C C     . VAL A 1 192 ? -33.351 -14.461 7.717   1.00 12.60 ? 192  VAL A C     1 
ATOM   1389 O O     . VAL A 1 192 ? -32.532 -15.042 8.416   1.00 14.00 ? 192  VAL A O     1 
ATOM   1390 C CB    . VAL A 1 192 ? -35.216 -15.921 6.772   1.00 15.22 ? 192  VAL A CB    1 
ATOM   1391 C CG1   . VAL A 1 192 ? -34.153 -16.995 6.617   1.00 17.15 ? 192  VAL A CG1   1 
ATOM   1392 C CG2   . VAL A 1 192 ? -36.553 -16.542 7.118   1.00 15.61 ? 192  VAL A CG2   1 
ATOM   1393 N N     . ARG A 1 193 ? -32.995 -13.481 6.880   1.00 12.00 ? 193  ARG A N     1 
ATOM   1394 C CA    . ARG A 1 193 ? -31.615 -13.062 6.735   1.00 11.53 ? 193  ARG A CA    1 
ATOM   1395 C C     . ARG A 1 193 ? -31.291 -12.020 7.809   1.00 11.06 ? 193  ARG A C     1 
ATOM   1396 O O     . ARG A 1 193 ? -31.093 -10.828 7.546   1.00 13.18 ? 193  ARG A O     1 
ATOM   1397 C CB    . ARG A 1 193 ? -31.421 -12.621 5.279   1.00 12.27 ? 193  ARG A CB    1 
ATOM   1398 C CG    . ARG A 1 193 ? -31.573 -13.751 4.264   1.00 13.17 ? 193  ARG A CG    1 
ATOM   1399 C CD    . ARG A 1 193 ? -30.859 -13.445 2.995   1.00 15.19 ? 193  ARG A CD    1 
ATOM   1400 N NE    . ARG A 1 193 ? -31.352 -12.240 2.336   1.00 15.35 ? 193  ARG A NE    1 
ATOM   1401 C CZ    . ARG A 1 193 ? -30.702 -11.610 1.347   1.00 16.96 ? 193  ARG A CZ    1 
ATOM   1402 N NH1   . ARG A 1 193 ? -29.464 -11.967 1.023   1.00 17.89 ? 193  ARG A NH1   1 
ATOM   1403 N NH2   . ARG A 1 193 ? -31.260 -10.583 0.724   1.00 15.24 ? 193  ARG A NH2   1 
ATOM   1404 N N     . GLY A 1 194 ? -31.236 -12.503 9.055   1.00 11.07 ? 194  GLY A N     1 
ATOM   1405 C CA    . GLY A 1 194 ? -30.761 -11.707 10.173  1.00 10.65 ? 194  GLY A CA    1 
ATOM   1406 C C     . GLY A 1 194 ? -31.614 -11.887 11.422  1.00 11.34 ? 194  GLY A C     1 
ATOM   1407 O O     . GLY A 1 194 ? -31.156 -11.498 12.488  1.00 12.14 ? 194  GLY A O     1 
ATOM   1408 N N     . ALA A 1 195 ? -32.838 -12.433 11.273  1.00 11.27 ? 195  ALA A N     1 
ATOM   1409 C CA    . ALA A 1 195 ? -33.794 -12.541 12.383  1.00 12.70 ? 195  ALA A CA    1 
ATOM   1410 C C     . ALA A 1 195 ? -34.645 -13.811 12.323  1.00 11.56 ? 195  ALA A C     1 
ATOM   1411 O O     . ALA A 1 195 ? -35.728 -13.849 12.910  1.00 13.13 ? 195  ALA A O     1 
ATOM   1412 C CB    . ALA A 1 195 ? -34.677 -11.321 12.432  1.00 12.76 ? 195  ALA A CB    1 
ATOM   1413 N N     . ALA A 1 196 ? -34.117 -14.904 11.748  1.00 12.40 ? 196  ALA A N     1 
ATOM   1414 C CA    . ALA A 1 196 ? -34.918 -16.084 11.491  1.00 12.46 ? 196  ALA A CA    1 
ATOM   1415 C C     . ALA A 1 196 ? -35.506 -16.634 12.790  1.00 12.17 ? 196  ALA A C     1 
ATOM   1416 O O     . ALA A 1 196 ? -36.603 -17.178 12.819  1.00 11.99 ? 196  ALA A O     1 
ATOM   1417 C CB    . ALA A 1 196 ? -34.110 -17.129 10.786  1.00 13.19 ? 196  ALA A CB    1 
ATOM   1418 N N     . SER A 1 197 ? -34.695 -16.620 13.859  1.00 11.63 ? 197  SER A N     1 
ATOM   1419 C CA    . SER A 1 197 ? -35.073 -17.206 15.145  1.00 11.05 ? 197  SER A CA    1 
ATOM   1420 C C     . SER A 1 197 ? -36.397 -16.673 15.706  1.00 12.06 ? 197  SER A C     1 
ATOM   1421 O O     . SER A 1 197 ? -37.048 -17.390 16.475  1.00 11.71 ? 197  SER A O     1 
ATOM   1422 C CB    . SER A 1 197 ? -33.939 -17.014 16.155  1.00 10.76 ? 197  SER A CB    1 
ATOM   1423 O OG    . SER A 1 197 ? -33.770 -15.629 16.446  1.00 11.23 ? 197  SER A OG    1 
ATOM   1424 N N     . SER A 1 198 ? -36.834 -15.477 15.277  1.00 12.60 ? 198  SER A N     1 
ATOM   1425 C CA    . SER A 1 198 ? -38.100 -14.883 15.691  1.00 12.53 ? 198  SER A CA    1 
ATOM   1426 C C     . SER A 1 198 ? -39.254 -15.256 14.768  1.00 12.29 ? 198  SER A C     1 
ATOM   1427 O O     . SER A 1 198 ? -40.383 -14.981 15.144  1.00 12.61 ? 198  SER A O     1 
ATOM   1428 C CB    . SER A 1 198 ? -38.008 -13.356 15.749  1.00 12.78 ? 198  SER A CB    1 
ATOM   1429 O OG    . SER A 1 198 ? -37.182 -12.947 16.830  1.00 13.31 ? 198  SER A OG    1 
ATOM   1430 N N     . VAL A 1 199 ? -39.009 -15.856 13.591  1.00 11.95 ? 199  VAL A N     1 
ATOM   1431 C CA    . VAL A 1 199 ? -40.106 -15.988 12.625  1.00 11.30 ? 199  VAL A CA    1 
ATOM   1432 C C     . VAL A 1 199 ? -40.355 -17.400 12.080  1.00 11.78 ? 199  VAL A C     1 
ATOM   1433 O O     . VAL A 1 199 ? -41.409 -17.640 11.491  1.00 12.85 ? 199  VAL A O     1 
ATOM   1434 C CB    . VAL A 1 199 ? -39.974 -14.994 11.462  1.00 12.28 ? 199  VAL A CB    1 
ATOM   1435 C CG1   . VAL A 1 199 ? -40.127 -13.562 11.955  1.00 13.33 ? 199  VAL A CG1   1 
ATOM   1436 C CG2   . VAL A 1 199 ? -38.695 -15.175 10.660  1.00 12.64 ? 199  VAL A CG2   1 
ATOM   1437 N N     . GLY A 1 200 ? -39.403 -18.327 12.165  1.00 11.99 ? 200  GLY A N     1 
ATOM   1438 C CA    . GLY A 1 200 ? -39.670 -19.655 11.655  1.00 11.95 ? 200  GLY A CA    1 
ATOM   1439 C C     . GLY A 1 200 ? -38.441 -20.532 11.765  1.00 12.69 ? 200  GLY A C     1 
ATOM   1440 O O     . GLY A 1 200 ? -37.421 -20.090 12.261  1.00 14.19 ? 200  GLY A O     1 
ATOM   1441 N N     . ILE A 1 201 ? -38.566 -21.794 11.355  1.00 11.87 ? 201  ILE A N     1 
ATOM   1442 C CA    . ILE A 1 201 ? -37.430 -22.684 11.390  1.00 11.35 ? 201  ILE A CA    1 
ATOM   1443 C C     . ILE A 1 201 ? -36.961 -22.922 9.949   1.00 11.65 ? 201  ILE A C     1 
ATOM   1444 O O     . ILE A 1 201 ? -37.701 -23.487 9.122   1.00 12.40 ? 201  ILE A O     1 
ATOM   1445 C CB    . ILE A 1 201 ? -37.759 -23.995 12.122  1.00 11.70 ? 201  ILE A CB    1 
ATOM   1446 C CG1   . ILE A 1 201 ? -38.235 -23.736 13.563  1.00 12.28 ? 201  ILE A CG1   1 
ATOM   1447 C CG2   . ILE A 1 201 ? -36.581 -24.963 12.057  1.00 13.05 ? 201  ILE A CG2   1 
ATOM   1448 C CD1   . ILE A 1 201 ? -38.563 -24.999 14.356  1.00 12.05 ? 201  ILE A CD1   1 
ATOM   1449 N N     . VAL A 1 202 ? -35.717 -22.535 9.684   1.00 11.70 ? 202  VAL A N     1 
ATOM   1450 C CA    . VAL A 1 202 ? -35.123 -22.747 8.376   1.00 11.77 ? 202  VAL A CA    1 
ATOM   1451 C C     . VAL A 1 202 ? -34.696 -24.217 8.274   1.00 12.17 ? 202  VAL A C     1 
ATOM   1452 O O     . VAL A 1 202 ? -33.881 -24.660 9.086   1.00 11.54 ? 202  VAL A O     1 
ATOM   1453 C CB    . VAL A 1 202 ? -33.971 -21.782 8.050   1.00 12.76 ? 202  VAL A CB    1 
ATOM   1454 C CG1   . VAL A 1 202 ? -33.343 -22.101 6.683   1.00 13.67 ? 202  VAL A CG1   1 
ATOM   1455 C CG2   . VAL A 1 202 ? -34.398 -20.336 8.082   1.00 14.09 ? 202  VAL A CG2   1 
ATOM   1456 N N     . THR A 1 203 ? -35.204 -24.939 7.269   1.00 11.86 ? 203  THR A N     1 
ATOM   1457 C CA    . THR A 1 203 ? -34.946 -26.370 7.135   1.00 11.40 ? 203  THR A CA    1 
ATOM   1458 C C     . THR A 1 203 ? -34.059 -26.718 5.934   1.00 11.86 ? 203  THR A C     1 
ATOM   1459 O O     . THR A 1 203 ? -33.627 -27.875 5.761   1.00 12.36 ? 203  THR A O     1 
ATOM   1460 C CB    . THR A 1 203 ? -36.269 -27.139 7.100   1.00 12.34 ? 203  THR A CB    1 
ATOM   1461 O OG1   . THR A 1 203 ? -37.109 -26.566 6.109   1.00 13.54 ? 203  THR A OG1   1 
ATOM   1462 C CG2   . THR A 1 203 ? -36.997 -27.061 8.423   1.00 12.32 ? 203  THR A CG2   1 
ATOM   1463 N N     . ASP A 1 204 ? -33.804 -25.722 5.094   1.00 12.06 ? 204  ASP A N     1 
ATOM   1464 C CA    . ASP A 1 204 ? -32.929 -25.896 3.954   1.00 11.65 ? 204  ASP A CA    1 
ATOM   1465 C C     . ASP A 1 204 ? -32.465 -24.533 3.476   1.00 12.04 ? 204  ASP A C     1 
ATOM   1466 O O     . ASP A 1 204 ? -33.208 -23.560 3.518   1.00 13.24 ? 204  ASP A O     1 
ATOM   1467 C CB    . ASP A 1 204 ? -33.664 -26.577 2.822   1.00 12.13 ? 204  ASP A CB    1 
ATOM   1468 C CG    . ASP A 1 204 ? -32.750 -27.148 1.758   1.00 17.05 ? 204  ASP A CG    1 
ATOM   1469 O OD1   . ASP A 1 204 ? -31.605 -27.480 2.108   1.00 18.78 ? 204  ASP A OD1   1 
ATOM   1470 O OD2   . ASP A 1 204 ? -33.200 -27.257 0.609   1.00 22.24 ? 204  ASP A OD2   1 
ATOM   1471 N N     . PHE A 1 205 ? -31.222 -24.481 3.009   1.00 11.76 ? 205  PHE A N     1 
ATOM   1472 C CA    . PHE A 1 205 ? -30.638 -23.268 2.448   1.00 12.54 ? 205  PHE A CA    1 
ATOM   1473 C C     . PHE A 1 205 ? -30.064 -23.573 1.059   1.00 14.21 ? 205  PHE A C     1 
ATOM   1474 O O     . PHE A 1 205 ? -29.409 -24.591 0.883   1.00 14.29 ? 205  PHE A O     1 
ATOM   1475 C CB    . PHE A 1 205 ? -29.424 -22.796 3.259   1.00 11.45 ? 205  PHE A CB    1 
ATOM   1476 C CG    . PHE A 1 205 ? -29.664 -22.345 4.699   1.00 11.81 ? 205  PHE A CG    1 
ATOM   1477 C CD1   . PHE A 1 205 ? -29.657 -23.259 5.733   1.00 12.23 ? 205  PHE A CD1   1 
ATOM   1478 C CD2   . PHE A 1 205 ? -29.883 -21.013 4.995   1.00 12.90 ? 205  PHE A CD2   1 
ATOM   1479 C CE1   . PHE A 1 205 ? -29.893 -22.845 7.025   1.00 11.88 ? 205  PHE A CE1   1 
ATOM   1480 C CE2   . PHE A 1 205 ? -30.104 -20.600 6.296   1.00 13.01 ? 205  PHE A CE2   1 
ATOM   1481 C CZ    . PHE A 1 205 ? -30.076 -21.531 7.322   1.00 11.71 ? 205  PHE A CZ    1 
ATOM   1482 N N     . SER A 1 206 ? -30.252 -22.635 0.121   1.00 14.20 ? 206  SER A N     1 
ATOM   1483 C CA    . SER A 1 206 ? -29.478 -22.556 -1.121  1.00 13.79 ? 206  SER A CA    1 
ATOM   1484 C C     . SER A 1 206 ? -28.498 -21.426 -1.003  1.00 12.89 ? 206  SER A C     1 
ATOM   1485 O O     . SER A 1 206 ? -28.945 -20.283 -0.862  1.00 13.12 ? 206  SER A O     1 
ATOM   1486 C CB    . SER A 1 206 ? -30.369 -22.271 -2.285  1.00 16.32 ? 206  SER A CB    1 
ATOM   1487 O OG    . SER A 1 206 ? -31.313 -23.318 -2.392  1.00 21.82 ? 206  SER A OG    1 
ATOM   1488 N N     . ILE A 1 207 ? -27.192 -21.755 -1.111  1.00 12.14 ? 207  ILE A N     1 
ATOM   1489 C CA    . ILE A 1 207 ? -26.138 -20.805 -0.837  1.00 12.63 ? 207  ILE A CA    1 
ATOM   1490 C C     . ILE A 1 207 ? -25.188 -20.772 -2.030  1.00 12.65 ? 207  ILE A C     1 
ATOM   1491 O O     . ILE A 1 207 ? -24.632 -21.806 -2.410  1.00 12.85 ? 207  ILE A O     1 
ATOM   1492 C CB    . ILE A 1 207 ? -25.383 -21.142 0.454   1.00 12.08 ? 207  ILE A CB    1 
ATOM   1493 C CG1   . ILE A 1 207 ? -26.385 -21.302 1.633   1.00 13.15 ? 207  ILE A CG1   1 
ATOM   1494 C CG2   . ILE A 1 207 ? -24.340 -20.069 0.703   1.00 12.70 ? 207  ILE A CG2   1 
ATOM   1495 C CD1   . ILE A 1 207 ? -25.730 -21.307 2.993   1.00 13.81 ? 207  ILE A CD1   1 
ATOM   1496 N N     . ARG A 1 208 ? -25.087 -19.577 -2.626  1.00 12.52 ? 208  ARG A N     1 
ATOM   1497 C CA    . ARG A 1 208 ? -24.111 -19.351 -3.683  1.00 13.23 ? 208  ARG A CA    1 
ATOM   1498 C C     . ARG A 1 208 ? -22.698 -19.440 -3.129  1.00 13.68 ? 208  ARG A C     1 
ATOM   1499 O O     . ARG A 1 208 ? -22.464 -19.162 -1.960  1.00 12.79 ? 208  ARG A O     1 
ATOM   1500 C CB    . ARG A 1 208 ? -24.362 -17.977 -4.308  1.00 15.66 ? 208  ARG A CB    1 
ATOM   1501 C CG    . ARG A 1 208 ? -25.692 -17.797 -5.012  1.00 20.90 ? 208  ARG A CG    1 
ATOM   1502 C CD    . ARG A 1 208 ? -25.855 -16.389 -5.578  1.00 26.35 ? 208  ARG A CD    1 
ATOM   1503 N NE    . ARG A 1 208 ? -25.568 -15.312 -4.602  1.00 33.62 ? 208  ARG A NE    1 
ATOM   1504 C CZ    . ARG A 1 208 ? -24.420 -14.603 -4.561  1.00 33.51 ? 208  ARG A CZ    1 
ATOM   1505 N NH1   . ARG A 1 208 ? -23.423 -14.850 -5.425  1.00 31.69 ? 208  ARG A NH1   1 
ATOM   1506 N NH2   . ARG A 1 208 ? -24.270 -13.647 -3.653  1.00 34.41 ? 208  ARG A NH2   1 
ATOM   1507 N N     . THR A 1 209 ? -21.714 -19.711 -4.012  1.00 12.95 ? 209  THR A N     1 
ATOM   1508 C CA    . THR A 1 209 ? -20.340 -19.841 -3.569  1.00 12.77 ? 209  THR A CA    1 
ATOM   1509 C C     . THR A 1 209 ? -19.395 -19.087 -4.497  1.00 13.19 ? 209  THR A C     1 
ATOM   1510 O O     . THR A 1 209 ? -19.730 -18.770 -5.640  1.00 14.65 ? 209  THR A O     1 
ATOM   1511 C CB    . THR A 1 209 ? -19.930 -21.311 -3.506  1.00 13.22 ? 209  THR A CB    1 
ATOM   1512 O OG1   . THR A 1 209 ? -19.799 -21.875 -4.812  1.00 13.83 ? 209  THR A OG1   1 
ATOM   1513 C CG2   . THR A 1 209 ? -20.880 -22.137 -2.662  1.00 13.29 ? 209  THR A CG2   1 
ATOM   1514 N N     . GLU A 1 210 ? -18.194 -18.892 -3.983  1.00 12.13 ? 210  GLU A N     1 
ATOM   1515 C CA    . GLU A 1 210 ? -17.080 -18.314 -4.708  1.00 13.06 ? 210  GLU A CA    1 
ATOM   1516 C C     . GLU A 1 210 ? -16.026 -19.399 -4.862  1.00 11.87 ? 210  GLU A C     1 
ATOM   1517 O O     . GLU A 1 210 ? -15.867 -20.301 -4.030  1.00 12.17 ? 210  GLU A O     1 
ATOM   1518 C CB    . GLU A 1 210 ? -16.459 -17.183 -3.875  1.00 14.41 ? 210  GLU A CB    1 
ATOM   1519 C CG    . GLU A 1 210 ? -17.397 -15.996 -3.697  1.00 14.76 ? 210  GLU A CG    1 
ATOM   1520 C CD    . GLU A 1 210 ? -17.631 -15.174 -4.953  1.00 17.02 ? 210  GLU A CD    1 
ATOM   1521 O OE1   . GLU A 1 210 ? -18.466 -14.254 -4.894  1.00 16.47 ? 210  GLU A OE1   1 
ATOM   1522 O OE2   . GLU A 1 210 ? -16.906 -15.411 -5.953  1.00 17.10 ? 210  GLU A OE2   1 
ATOM   1523 N N     . PRO A 1 211 ? -15.153 -19.277 -5.892  1.00 12.54 ? 211  PRO A N     1 
ATOM   1524 C CA    . PRO A 1 211 ? -13.942 -20.082 -5.930  1.00 12.24 ? 211  PRO A CA    1 
ATOM   1525 C C     . PRO A 1 211 ? -13.076 -19.684 -4.750  1.00 11.84 ? 211  PRO A C     1 
ATOM   1526 O O     . PRO A 1 211 ? -13.012 -18.519 -4.408  1.00 13.65 ? 211  PRO A O     1 
ATOM   1527 C CB    . PRO A 1 211 ? -13.299 -19.690 -7.272  1.00 12.48 ? 211  PRO A CB    1 
ATOM   1528 C CG    . PRO A 1 211 ? -13.800 -18.275 -7.488  1.00 13.64 ? 211  PRO A CG    1 
ATOM   1529 C CD    . PRO A 1 211 ? -15.202 -18.245 -6.934  1.00 12.65 ? 211  PRO A CD    1 
ATOM   1530 N N     . VAL A 1 212 ? -12.381 -20.638 -4.139  1.00 12.24 ? 212  VAL A N     1 
ATOM   1531 C CA    . VAL A 1 212 ? -11.445 -20.307 -3.088  1.00 13.97 ? 212  VAL A CA    1 
ATOM   1532 C C     . VAL A 1 212 ? -10.357 -19.366 -3.594  1.00 14.98 ? 212  VAL A C     1 
ATOM   1533 O O     . VAL A 1 212 ? -9.984  -19.360 -4.774  1.00 14.24 ? 212  VAL A O     1 
ATOM   1534 C CB    . VAL A 1 212 ? -10.838 -21.555 -2.421  1.00 14.05 ? 212  VAL A CB    1 
ATOM   1535 C CG1   . VAL A 1 212 ? -11.917 -22.375 -1.710  1.00 13.87 ? 212  VAL A CG1   1 
ATOM   1536 C CG2   . VAL A 1 212 ? -10.037 -22.419 -3.406  1.00 14.48 ? 212  VAL A CG2   1 
ATOM   1537 N N     . PRO A 1 213 ? -9.749  -18.572 -2.687  1.00 15.10 ? 213  PRO A N     1 
ATOM   1538 C CA    . PRO A 1 213 ? -8.578  -17.775 -3.063  1.00 15.52 ? 213  PRO A CA    1 
ATOM   1539 C C     . PRO A 1 213 ? -7.390  -18.676 -3.422  1.00 14.90 ? 213  PRO A C     1 
ATOM   1540 O O     . PRO A 1 213 ? -7.197  -19.746 -2.850  1.00 15.66 ? 213  PRO A O     1 
ATOM   1541 C CB    . PRO A 1 213 ? -8.277  -16.891 -1.842  1.00 16.31 ? 213  PRO A CB    1 
ATOM   1542 C CG    . PRO A 1 213 ? -9.396  -17.175 -0.847  1.00 16.10 ? 213  PRO A CG    1 
ATOM   1543 C CD    . PRO A 1 213 ? -10.134 -18.441 -1.272  1.00 15.36 ? 213  PRO A CD    1 
ATOM   1544 N N     . VAL A 1 214 ? -6.577  -18.223 -4.379  1.00 16.64 ? 214  VAL A N     1 
ATOM   1545 C CA    . VAL A 1 214 ? -5.376  -18.957 -4.736  1.00 17.76 ? 214  VAL A CA    1 
ATOM   1546 C C     . VAL A 1 214 ? -4.412  -19.038 -3.559  1.00 16.98 ? 214  VAL A C     1 
ATOM   1547 O O     . VAL A 1 214 ? -3.791  -20.070 -3.319  1.00 17.49 ? 214  VAL A O     1 
ATOM   1548 C CB    . VAL A 1 214 ? -4.743  -18.268 -5.958  1.00 19.72 ? 214  VAL A CB    1 
ATOM   1549 C CG1   . VAL A 1 214 ? -3.333  -18.761 -6.196  1.00 21.16 ? 214  VAL A CG1   1 
ATOM   1550 C CG2   . VAL A 1 214 ? -5.622  -18.466 -7.193  1.00 23.12 ? 214  VAL A CG2   1 
ATOM   1551 N N     . SER A 1 215 ? -4.335  -17.937 -2.812  1.00 17.34 ? 215  SER A N     1 
ATOM   1552 C CA    . SER A 1 215 ? -3.399  -17.808 -1.711  1.00 19.11 ? 215  SER A CA    1 
ATOM   1553 C C     . SER A 1 215 ? -4.094  -17.117 -0.539  1.00 16.53 ? 215  SER A C     1 
ATOM   1554 O O     . SER A 1 215 ? -4.699  -16.056 -0.738  1.00 17.94 ? 215  SER A O     1 
ATOM   1555 C CB    . SER A 1 215 ? -2.207  -17.009 -2.160  1.00 20.50 ? 215  SER A CB    1 
ATOM   1556 O OG    . SER A 1 215 ? -1.224  -16.901 -1.134  1.00 25.67 ? 215  SER A OG    1 
ATOM   1557 N N     . SER A 1 216 ? -3.928  -17.702 0.650   1.00 17.00 ? 216  SER A N     1 
ATOM   1558 C CA    . SER A 1 216 ? -4.425  -17.158 1.912   1.00 15.76 ? 216  SER A CA    1 
ATOM   1559 C C     . SER A 1 216 ? -3.273  -17.045 2.905   1.00 16.26 ? 216  SER A C     1 
ATOM   1560 O O     . SER A 1 216 ? -2.703  -18.051 3.278   1.00 19.25 ? 216  SER A O     1 
ATOM   1561 C CB    . SER A 1 216 ? -5.542  -18.024 2.474   1.00 16.24 ? 216  SER A CB    1 
ATOM   1562 O OG    . SER A 1 216 ? -6.568  -18.167 1.487   1.00 15.75 ? 216  SER A OG    1 
ATOM   1563 N N     . VAL A 1 217 ? -2.994  -15.818 3.330   1.00 15.56 ? 217  VAL A N     1 
ATOM   1564 C CA    . VAL A 1 217 ? -1.887  -15.530 4.230   1.00 17.97 ? 217  VAL A CA    1 
ATOM   1565 C C     . VAL A 1 217 ? -2.441  -15.110 5.583   1.00 19.71 ? 217  VAL A C     1 
ATOM   1566 O O     . VAL A 1 217 ? -3.110  -14.080 5.653   1.00 21.52 ? 217  VAL A O     1 
ATOM   1567 C CB    . VAL A 1 217 ? -1.001  -14.421 3.664   1.00 20.12 ? 217  VAL A CB    1 
ATOM   1568 C CG1   . VAL A 1 217 ? 0.150   -14.086 4.620   1.00 23.65 ? 217  VAL A CG1   1 
ATOM   1569 C CG2   . VAL A 1 217 ? -0.483  -14.796 2.290   1.00 21.50 ? 217  VAL A CG2   1 
ATOM   1570 N N     . THR A 1 218 ? -2.158  -15.899 6.628   1.00 18.84 ? 218  THR A N     1 
ATOM   1571 C CA    . THR A 1 218 ? -2.516  -15.502 7.984   1.00 18.43 ? 218  THR A CA    1 
ATOM   1572 C C     . THR A 1 218 ? -1.397  -14.644 8.560   1.00 20.93 ? 218  THR A C     1 
ATOM   1573 O O     . THR A 1 218 ? -0.212  -14.914 8.331   1.00 20.55 ? 218  THR A O     1 
ATOM   1574 C CB    . THR A 1 218 ? -2.795  -16.685 8.901   1.00 20.24 ? 218  THR A CB    1 
ATOM   1575 O OG1   . THR A 1 218 ? -1.589  -17.448 9.014   1.00 25.20 ? 218  THR A OG1   1 
ATOM   1576 C CG2   . THR A 1 218 ? -3.934  -17.536 8.371   1.00 18.88 ? 218  THR A CG2   1 
ATOM   1577 N N     . TYR A 1 219 ? -1.778  -13.565 9.242   1.00 18.72 ? 219  TYR A N     1 
ATOM   1578 C CA    . TYR A 1 219 ? -0.773  -12.805 9.980   1.00 17.04 ? 219  TYR A CA    1 
ATOM   1579 C C     . TYR A 1 219 ? -1.188  -12.579 11.427  1.00 16.77 ? 219  TYR A C     1 
ATOM   1580 O O     . TYR A 1 219 ? -2.368  -12.560 11.774  1.00 17.07 ? 219  TYR A O     1 
ATOM   1581 C CB    . TYR A 1 219 ? -0.540  -11.502 9.242   1.00 16.99 ? 219  TYR A CB    1 
ATOM   1582 C CG    . TYR A 1 219 ? -1.718  -10.543 9.238   1.00 16.52 ? 219  TYR A CG    1 
ATOM   1583 C CD1   . TYR A 1 219 ? -1.893  -9.592  10.239  1.00 14.72 ? 219  TYR A CD1   1 
ATOM   1584 C CD2   . TYR A 1 219 ? -2.641  -10.578 8.197   1.00 15.16 ? 219  TYR A CD2   1 
ATOM   1585 C CE1   . TYR A 1 219 ? -2.924  -8.667  10.188  1.00 14.32 ? 219  TYR A CE1   1 
ATOM   1586 C CE2   . TYR A 1 219 ? -3.686  -9.674  8.140   1.00 15.53 ? 219  TYR A CE2   1 
ATOM   1587 C CZ    . TYR A 1 219 ? -3.827  -8.716  9.138   1.00 15.64 ? 219  TYR A CZ    1 
ATOM   1588 O OH    . TYR A 1 219 ? -4.852  -7.830  9.125   1.00 14.66 ? 219  TYR A OH    1 
ATOM   1589 N N     . SER A 1 220 ? -0.169  -12.361 12.267  1.00 17.58 ? 220  SER A N     1 
ATOM   1590 C CA    . SER A 1 220 ? -0.369  -12.083 13.671  1.00 19.60 ? 220  SER A CA    1 
ATOM   1591 C C     . SER A 1 220 ? 0.845   -11.307 14.168  1.00 18.92 ? 220  SER A C     1 
ATOM   1592 O O     . SER A 1 220 ? 1.975   -11.762 14.011  1.00 19.98 ? 220  SER A O     1 
ATOM   1593 C CB    . SER A 1 220 ? -0.546  -13.382 14.421  1.00 24.47 ? 220  SER A CB    1 
ATOM   1594 O OG    . SER A 1 220 ? -0.518  -13.135 15.808  1.00 32.32 ? 220  SER A OG    1 
ATOM   1595 N N     . TYR A 1 221 ? 0.598   -10.106 14.695  1.00 16.07 ? 221  TYR A N     1 
ATOM   1596 C CA    . TYR A 1 221 ? 1.616   -9.277  15.309  1.00 17.21 ? 221  TYR A CA    1 
ATOM   1597 C C     . TYR A 1 221 ? 1.259   -9.076  16.787  1.00 17.79 ? 221  TYR A C     1 
ATOM   1598 O O     . TYR A 1 221 ? 0.153   -8.654  17.101  1.00 15.00 ? 221  TYR A O     1 
ATOM   1599 C CB    . TYR A 1 221 ? 1.629   -7.909  14.649  1.00 16.62 ? 221  TYR A CB    1 
ATOM   1600 C CG    . TYR A 1 221 ? 1.989   -7.951  13.170  1.00 18.29 ? 221  TYR A CG    1 
ATOM   1601 C CD1   . TYR A 1 221 ? 3.302   -8.127  12.770  1.00 20.70 ? 221  TYR A CD1   1 
ATOM   1602 C CD2   . TYR A 1 221 ? 1.016   -7.833  12.189  1.00 18.63 ? 221  TYR A CD2   1 
ATOM   1603 C CE1   . TYR A 1 221 ? 3.657   -8.136  11.435  1.00 20.51 ? 221  TYR A CE1   1 
ATOM   1604 C CE2   . TYR A 1 221 ? 1.351   -7.872  10.846  1.00 21.25 ? 221  TYR A CE2   1 
ATOM   1605 C CZ    . TYR A 1 221 ? 2.673   -8.024  10.472  1.00 23.75 ? 221  TYR A CZ    1 
ATOM   1606 O OH    . TYR A 1 221 ? 2.984   -8.033  9.147   1.00 21.76 ? 221  TYR A OH    1 
ATOM   1607 N N     . ILE A 1 222 ? 2.182   -9.401  17.696  1.00 15.94 ? 222  ILE A N     1 
ATOM   1608 C CA    . ILE A 1 222 ? 1.861   -9.424  19.111  1.00 16.73 ? 222  ILE A CA    1 
ATOM   1609 C C     . ILE A 1 222 ? 2.687   -8.375  19.847  1.00 16.69 ? 222  ILE A C     1 
ATOM   1610 O O     . ILE A 1 222 ? 3.898   -8.356  19.689  1.00 16.80 ? 222  ILE A O     1 
ATOM   1611 C CB    . ILE A 1 222 ? 2.138   -10.810 19.708  1.00 18.06 ? 222  ILE A CB    1 
ATOM   1612 C CG1   . ILE A 1 222 ? 1.390   -11.915 18.954  1.00 19.95 ? 222  ILE A CG1   1 
ATOM   1613 C CG2   . ILE A 1 222 ? 1.850   -10.815 21.207  1.00 18.52 ? 222  ILE A CG2   1 
ATOM   1614 C CD1   . ILE A 1 222 ? 1.795   -13.311 19.402  1.00 23.89 ? 222  ILE A CD1   1 
ATOM   1615 N N     . TRP A 1 223 ? 2.028   -7.553  20.665  1.00 15.25 ? 223  TRP A N     1 
ATOM   1616 C CA    . TRP A 1 223 ? 2.700   -6.682  21.617  1.00 16.61 ? 223  TRP A CA    1 
ATOM   1617 C C     . TRP A 1 223 ? 2.442   -7.233  23.013  1.00 17.22 ? 223  TRP A C     1 
ATOM   1618 O O     . TRP A 1 223 ? 1.292   -7.356  23.415  1.00 16.07 ? 223  TRP A O     1 
ATOM   1619 C CB    . TRP A 1 223 ? 2.171   -5.248  21.539  1.00 16.11 ? 223  TRP A CB    1 
ATOM   1620 C CG    . TRP A 1 223 ? 2.445   -4.515  20.254  1.00 18.08 ? 223  TRP A CG    1 
ATOM   1621 C CD1   . TRP A 1 223 ? 3.364   -3.514  20.105  1.00 20.46 ? 223  TRP A CD1   1 
ATOM   1622 C CD2   . TRP A 1 223 ? 1.718   -4.576  19.000  1.00 17.37 ? 223  TRP A CD2   1 
ATOM   1623 N NE1   . TRP A 1 223 ? 3.340   -3.026  18.827  1.00 19.09 ? 223  TRP A NE1   1 
ATOM   1624 C CE2   . TRP A 1 223 ? 2.335   -3.637  18.128  1.00 19.29 ? 223  TRP A CE2   1 
ATOM   1625 C CE3   . TRP A 1 223 ? 0.638   -5.311  18.515  1.00 16.90 ? 223  TRP A CE3   1 
ATOM   1626 C CZ2   . TRP A 1 223 ? 1.882   -3.411  16.825  1.00 18.62 ? 223  TRP A CZ2   1 
ATOM   1627 C CZ3   . TRP A 1 223 ? 0.188   -5.083  17.230  1.00 18.02 ? 223  TRP A CZ3   1 
ATOM   1628 C CH2   . TRP A 1 223 ? 0.804   -4.155  16.393  1.00 18.54 ? 223  TRP A CH2   1 
ATOM   1629 N N     . GLU A 1 224 ? 3.504   -7.545  23.745  1.00 15.94 ? 224  GLU A N     1 
ATOM   1630 C CA    . GLU A 1 224 ? 3.390   -8.119  25.073  1.00 18.59 ? 224  GLU A CA    1 
ATOM   1631 C C     . GLU A 1 224 ? 3.462   -6.994  26.104  1.00 17.00 ? 224  GLU A C     1 
ATOM   1632 O O     . GLU A 1 224 ? 4.183   -6.015  25.923  1.00 19.09 ? 224  GLU A O     1 
ATOM   1633 C CB    . GLU A 1 224 ? 4.546   -9.101  25.276  1.00 21.19 ? 224  GLU A CB    1 
ATOM   1634 C CG    . GLU A 1 224 ? 4.491   -10.294 24.328  1.00 26.36 ? 224  GLU A CG    1 
ATOM   1635 C CD    . GLU A 1 224 ? 5.773   -11.091 24.184  1.00 34.12 ? 224  GLU A CD    1 
ATOM   1636 O OE1   . GLU A 1 224 ? 6.810   -10.642 24.707  1.00 36.16 ? 224  GLU A OE1   1 
ATOM   1637 O OE2   . GLU A 1 224 ? 5.718   -12.169 23.549  1.00 46.74 ? 224  GLU A OE2   1 
ATOM   1638 N N     . GLY A 1 225 ? 2.663   -7.109  27.160  1.00 15.36 ? 225  GLY A N     1 
ATOM   1639 C CA    . GLY A 1 225 ? 2.812   -6.221  28.291  1.00 16.56 ? 225  GLY A CA    1 
ATOM   1640 C C     . GLY A 1 225 ? 1.476   -5.769  28.848  1.00 17.92 ? 225  GLY A C     1 
ATOM   1641 O O     . GLY A 1 225 ? 0.427   -6.070  28.278  1.00 18.06 ? 225  GLY A O     1 
ATOM   1642 N N     . THR A 1 226 ? 1.538   -5.047  29.975  1.00 15.47 ? 226  THR A N     1 
ATOM   1643 C CA    . THR A 1 226 ? 0.343   -4.645  30.694  1.00 16.07 ? 226  THR A CA    1 
ATOM   1644 C C     . THR A 1 226 ? 0.197   -3.131  30.742  1.00 15.57 ? 226  THR A C     1 
ATOM   1645 O O     . THR A 1 226 ? -0.720  -2.634  31.409  1.00 17.47 ? 226  THR A O     1 
ATOM   1646 C CB    . THR A 1 226 ? 0.329   -5.262  32.098  1.00 17.05 ? 226  THR A CB    1 
ATOM   1647 O OG1   . THR A 1 226 ? 1.487   -4.781  32.785  1.00 17.72 ? 226  THR A OG1   1 
ATOM   1648 C CG2   . THR A 1 226 ? 0.387   -6.780  32.027  1.00 18.47 ? 226  THR A CG2   1 
ATOM   1649 N N     . ASP A 1 227 ? 1.018   -2.393  30.003  1.00 17.27 ? 227  ASP A N     1 
ATOM   1650 C CA    . ASP A 1 227 ? 0.981   -0.943  30.149  1.00 17.34 ? 227  ASP A CA    1 
ATOM   1651 C C     . ASP A 1 227 ? -0.250  -0.401  29.433  1.00 17.76 ? 227  ASP A C     1 
ATOM   1652 O O     . ASP A 1 227 ? -0.319  -0.464  28.211  1.00 17.02 ? 227  ASP A O     1 
ATOM   1653 C CB    . ASP A 1 227 ? 2.252   -0.286  29.642  1.00 19.73 ? 227  ASP A CB    1 
ATOM   1654 C CG    . ASP A 1 227 ? 2.284   1.244   29.597  1.00 23.91 ? 227  ASP A CG    1 
ATOM   1655 O OD1   . ASP A 1 227 ? 1.331   1.889   30.059  1.00 30.47 ? 227  ASP A OD1   1 
ATOM   1656 O OD2   . ASP A 1 227 ? 3.288   1.794   29.117  1.00 29.80 ? 227  ASP A OD2   1 
ATOM   1657 N N     . PRO A 1 228 ? -1.234  0.199   30.139  1.00 16.07 ? 228  PRO A N     1 
ATOM   1658 C CA    . PRO A 1 228 ? -2.432  0.703   29.464  1.00 15.47 ? 228  PRO A CA    1 
ATOM   1659 C C     . PRO A 1 228 ? -2.174  1.768   28.408  1.00 15.90 ? 228  PRO A C     1 
ATOM   1660 O O     . PRO A 1 228 ? -2.863  1.797   27.393  1.00 15.84 ? 228  PRO A O     1 
ATOM   1661 C CB    . PRO A 1 228 ? -3.341  1.213   30.592  1.00 17.30 ? 228  PRO A CB    1 
ATOM   1662 C CG    . PRO A 1 228 ? -2.401  1.400   31.763  1.00 18.19 ? 228  PRO A CG    1 
ATOM   1663 C CD    . PRO A 1 228 ? -1.286  0.397   31.600  1.00 17.51 ? 228  PRO A CD    1 
ATOM   1664 N N     . ALA A 1 229 ? -1.188  2.646   28.608  1.00 16.91 ? 229  ALA A N     1 
ATOM   1665 C CA    . ALA A 1 229 ? -0.950  3.693   27.613  1.00 17.25 ? 229  ALA A CA    1 
ATOM   1666 C C     . ALA A 1 229 ? -0.420  3.078   26.317  1.00 17.77 ? 229  ALA A C     1 
ATOM   1667 O O     . ALA A 1 229 ? -0.843  3.502   25.228  1.00 18.38 ? 229  ALA A O     1 
ATOM   1668 C CB    . ALA A 1 229 ? -0.021  4.755   28.199  1.00 18.92 ? 229  ALA A CB    1 
ATOM   1669 N N     . ALA A 1 230 ? 0.463   2.076   26.433  1.00 15.91 ? 230  ALA A N     1 
ATOM   1670 C CA    . ALA A 1 230 ? 1.044   1.424   25.274  1.00 16.77 ? 230  ALA A CA    1 
ATOM   1671 C C     . ALA A 1 230 ? -0.046  0.657   24.509  1.00 17.62 ? 230  ALA A C     1 
ATOM   1672 O O     . ALA A 1 230 ? -0.103  0.694   23.267  1.00 16.54 ? 230  ALA A O     1 
ATOM   1673 C CB    . ALA A 1 230 ? 2.180   0.490   25.680  1.00 18.10 ? 230  ALA A CB    1 
ATOM   1674 N N     . ARG A 1 231 ? -0.923  -0.023  25.256  1.00 15.40 ? 231  ARG A N     1 
ATOM   1675 C CA    . ARG A 1 231 ? -2.036  -0.746  24.647  1.00 15.81 ? 231  ARG A CA    1 
ATOM   1676 C C     . ARG A 1 231 ? -3.030  0.191   23.959  1.00 15.80 ? 231  ARG A C     1 
ATOM   1677 O O     . ARG A 1 231 ? -3.536  -0.123  22.870  1.00 13.96 ? 231  ARG A O     1 
ATOM   1678 C CB    . ARG A 1 231 ? -2.686  -1.638  25.708  1.00 15.19 ? 231  ARG A CB    1 
ATOM   1679 C CG    . ARG A 1 231 ? -1.738  -2.760  26.144  1.00 14.05 ? 231  ARG A CG    1 
ATOM   1680 C CD    . ARG A 1 231 ? -2.015  -3.230  27.560  1.00 14.04 ? 231  ARG A CD    1 
ATOM   1681 N NE    . ARG A 1 231 ? -3.387  -3.698  27.783  1.00 14.01 ? 231  ARG A NE    1 
ATOM   1682 C CZ    . ARG A 1 231 ? -3.831  -4.919  27.550  1.00 15.34 ? 231  ARG A CZ    1 
ATOM   1683 N NH1   . ARG A 1 231 ? -3.101  -5.796  26.902  1.00 14.81 ? 231  ARG A NH1   1 
ATOM   1684 N NH2   . ARG A 1 231 ? -5.046  -5.274  27.947  1.00 16.31 ? 231  ARG A NH2   1 
ATOM   1685 N N     . ALA A 1 232 ? -3.347  1.335   24.584  1.00 15.78 ? 232  ALA A N     1 
ATOM   1686 C CA    . ALA A 1 232 ? -4.247  2.288   23.973  1.00 16.06 ? 232  ALA A CA    1 
ATOM   1687 C C     . ALA A 1 232 ? -3.663  2.821   22.673  1.00 16.89 ? 232  ALA A C     1 
ATOM   1688 O O     . ALA A 1 232 ? -4.414  3.052   21.739  1.00 16.58 ? 232  ALA A O     1 
ATOM   1689 C CB    . ALA A 1 232 ? -4.531  3.438   24.905  1.00 15.86 ? 232  ALA A CB    1 
ATOM   1690 N N     . GLU A 1 233 ? -2.338  3.000   22.636  1.00 17.44 ? 233  GLU A N     1 
ATOM   1691 C CA    . GLU A 1 233 ? -1.653  3.512   21.450  1.00 18.28 ? 233  GLU A CA    1 
ATOM   1692 C C     . GLU A 1 233 ? -1.805  2.516   20.296  1.00 16.84 ? 233  GLU A C     1 
ATOM   1693 O O     . GLU A 1 233 ? -2.095  2.933   19.173  1.00 17.28 ? 233  GLU A O     1 
ATOM   1694 C CB    . GLU A 1 233 ? -0.219  3.912   21.783  1.00 22.33 ? 233  GLU A CB    1 
ATOM   1695 C CG    . GLU A 1 233 ? 0.646   4.173   20.555  1.00 32.00 ? 233  GLU A CG    1 
ATOM   1696 C CD    . GLU A 1 233 ? 0.428   5.510   19.860  1.00 43.49 ? 233  GLU A CD    1 
ATOM   1697 O OE1   . GLU A 1 233 ? -0.410  6.325   20.346  1.00 54.64 ? 233  GLU A OE1   1 
ATOM   1698 O OE2   . GLU A 1 233 ? 1.121   5.741   18.824  1.00 52.08 ? 233  GLU A OE2   1 
ATOM   1699 N N     . VAL A 1 234 ? -1.669  1.223   20.591  1.00 14.47 ? 234  VAL A N     1 
ATOM   1700 C CA    . VAL A 1 234 ? -1.868  0.191   19.581  1.00 14.40 ? 234  VAL A CA    1 
ATOM   1701 C C     . VAL A 1 234 ? -3.313  0.238   19.061  1.00 14.39 ? 234  VAL A C     1 
ATOM   1702 O O     . VAL A 1 234 ? -3.579  0.254   17.860  1.00 13.43 ? 234  VAL A O     1 
ATOM   1703 C CB    . VAL A 1 234 ? -1.490  -1.197  20.120  1.00 14.69 ? 234  VAL A CB    1 
ATOM   1704 C CG1   . VAL A 1 234 ? -1.887  -2.298  19.154  1.00 14.80 ? 234  VAL A CG1   1 
ATOM   1705 C CG2   . VAL A 1 234 ? -0.007  -1.326  20.431  1.00 16.14 ? 234  VAL A CG2   1 
ATOM   1706 N N     . PHE A 1 235 ? -4.279  0.279   19.968  1.00 12.63 ? 235  PHE A N     1 
ATOM   1707 C CA    . PHE A 1 235 ? -5.669  0.374   19.579  1.00 12.63 ? 235  PHE A CA    1 
ATOM   1708 C C     . PHE A 1 235 ? -5.919  1.594   18.683  1.00 12.19 ? 235  PHE A C     1 
ATOM   1709 O O     . PHE A 1 235 ? -6.589  1.495   17.639  1.00 13.51 ? 235  PHE A O     1 
ATOM   1710 C CB    . PHE A 1 235 ? -6.607  0.416   20.799  1.00 12.46 ? 235  PHE A CB    1 
ATOM   1711 C CG    . PHE A 1 235 ? -8.026  0.766   20.376  1.00 13.60 ? 235  PHE A CG    1 
ATOM   1712 C CD1   . PHE A 1 235 ? -8.859  -0.194  19.796  1.00 14.96 ? 235  PHE A CD1   1 
ATOM   1713 C CD2   . PHE A 1 235 ? -8.509  2.075   20.463  1.00 14.47 ? 235  PHE A CD2   1 
ATOM   1714 C CE1   . PHE A 1 235 ? -10.108 0.143   19.288  1.00 14.68 ? 235  PHE A CE1   1 
ATOM   1715 C CE2   . PHE A 1 235 ? -9.775  2.393   20.013  1.00 14.81 ? 235  PHE A CE2   1 
ATOM   1716 C CZ    . PHE A 1 235 ? -10.560 1.444   19.398  1.00 14.98 ? 235  PHE A CZ    1 
ATOM   1717 N N     . LEU A 1 236 ? -5.449  2.776   19.126  1.00 13.78 ? 236  LEU A N     1 
ATOM   1718 C CA    . LEU A 1 236 ? -5.750  4.011   18.397  1.00 14.21 ? 236  LEU A CA    1 
ATOM   1719 C C     . LEU A 1 236 ? -5.165  3.971   16.986  1.00 13.90 ? 236  LEU A C     1 
ATOM   1720 O O     . LEU A 1 236 ? -5.784  4.438   16.020  1.00 14.54 ? 236  LEU A O     1 
ATOM   1721 C CB    . LEU A 1 236 ? -5.302  5.233   19.190  1.00 14.93 ? 236  LEU A CB    1 
ATOM   1722 C CG    . LEU A 1 236 ? -6.113  5.537   20.452  1.00 15.65 ? 236  LEU A CG    1 
ATOM   1723 C CD1   . LEU A 1 236 ? -5.417  6.549   21.342  1.00 16.79 ? 236  LEU A CD1   1 
ATOM   1724 C CD2   . LEU A 1 236 ? -7.506  6.018   20.065  1.00 16.25 ? 236  LEU A CD2   1 
ATOM   1725 N N     . THR A 1 237 ? -3.973  3.410   16.856  1.00 13.85 ? 237  THR A N     1 
ATOM   1726 C CA    . THR A 1 237 ? -3.350  3.244   15.552  1.00 15.38 ? 237  THR A CA    1 
ATOM   1727 C C     . THR A 1 237 ? -4.197  2.281   14.722  1.00 16.35 ? 237  THR A C     1 
ATOM   1728 O O     . THR A 1 237 ? -4.464  2.535   13.552  1.00 15.01 ? 237  THR A O     1 
ATOM   1729 C CB    . THR A 1 237 ? -1.910  2.743   15.686  1.00 17.06 ? 237  THR A CB    1 
ATOM   1730 O OG1   . THR A 1 237 ? -1.188  3.760   16.385  1.00 17.65 ? 237  THR A OG1   1 
ATOM   1731 C CG2   . THR A 1 237 ? -1.293  2.526   14.316  1.00 18.29 ? 237  THR A CG2   1 
ATOM   1732 N N     . TRP A 1 238 ? -4.603  1.157   15.345  1.00 16.64 ? 238  TRP A N     1 
ATOM   1733 C CA    . TRP A 1 238 ? -5.396  0.159   14.653  1.00 14.78 ? 238  TRP A CA    1 
ATOM   1734 C C     . TRP A 1 238 ? -6.668  0.794   14.088  1.00 13.38 ? 238  TRP A C     1 
ATOM   1735 O O     . TRP A 1 238 ? -7.017  0.598   12.910  1.00 16.02 ? 238  TRP A O     1 
ATOM   1736 C CB    . TRP A 1 238 ? -5.687  -1.016  15.612  1.00 13.36 ? 238  TRP A CB    1 
ATOM   1737 C CG    . TRP A 1 238 ? -6.562  -2.072  15.006  1.00 13.89 ? 238  TRP A CG    1 
ATOM   1738 C CD1   . TRP A 1 238 ? -6.122  -3.197  14.369  1.00 14.49 ? 238  TRP A CD1   1 
ATOM   1739 C CD2   . TRP A 1 238 ? -8.005  -2.125  14.962  1.00 13.84 ? 238  TRP A CD2   1 
ATOM   1740 N NE1   . TRP A 1 238 ? -7.182  -3.949  13.946  1.00 13.44 ? 238  TRP A NE1   1 
ATOM   1741 C CE2   . TRP A 1 238 ? -8.349  -3.315  14.282  1.00 13.83 ? 238  TRP A CE2   1 
ATOM   1742 C CE3   . TRP A 1 238 ? -9.037  -1.320  15.449  1.00 13.67 ? 238  TRP A CE3   1 
ATOM   1743 C CZ2   . TRP A 1 238 ? -9.682  -3.673  14.043  1.00 14.03 ? 238  TRP A CZ2   1 
ATOM   1744 C CZ3   . TRP A 1 238 ? -10.351 -1.677  15.227  1.00 13.66 ? 238  TRP A CZ3   1 
ATOM   1745 C CH2   . TRP A 1 238 ? -10.675 -2.843  14.529  1.00 13.76 ? 238  TRP A CH2   1 
ATOM   1746 N N     . GLN A 1 239 ? -7.331  1.596   14.912  1.00 14.29 ? 239  GLN A N     1 
ATOM   1747 C CA    . GLN A 1 239 ? -8.574  2.267   14.563  1.00 13.77 ? 239  GLN A CA    1 
ATOM   1748 C C     . GLN A 1 239 ? -8.353  3.307   13.460  1.00 15.46 ? 239  GLN A C     1 
ATOM   1749 O O     . GLN A 1 239 ? -9.143  3.373   12.529  1.00 17.15 ? 239  GLN A O     1 
ATOM   1750 C CB    . GLN A 1 239 ? -9.182  2.948   15.784  1.00 13.44 ? 239  GLN A CB    1 
ATOM   1751 C CG    . GLN A 1 239 ? -10.520 3.615   15.503  1.00 14.36 ? 239  GLN A CG    1 
ATOM   1752 C CD    . GLN A 1 239 ? -11.177 4.211   16.722  1.00 14.70 ? 239  GLN A CD    1 
ATOM   1753 O OE1   . GLN A 1 239 ? -12.302 3.864   17.100  1.00 14.73 ? 239  GLN A OE1   1 
ATOM   1754 N NE2   . GLN A 1 239 ? -10.468 5.161   17.319  1.00 14.85 ? 239  GLN A NE2   1 
ATOM   1755 N N     . SER A 1 240 ? -7.273  4.092   13.539  1.00 16.90 ? 240  SER A N     1 
ATOM   1756 C CA    A SER A 1 240 ? -7.105  5.160   12.563  0.50 16.96 ? 240  SER A CA    1 
ATOM   1757 C CA    B SER A 1 240 ? -7.007  5.160   12.584  0.50 18.31 ? 240  SER A CA    1 
ATOM   1758 C C     . SER A 1 240 ? -6.689  4.603   11.203  1.00 18.42 ? 240  SER A C     1 
ATOM   1759 O O     . SER A 1 240 ? -7.121  5.142   10.178  1.00 17.30 ? 240  SER A O     1 
ATOM   1760 C CB    A SER A 1 240 ? -6.159  6.224   13.027  0.50 17.97 ? 240  SER A CB    1 
ATOM   1761 C CB    B SER A 1 240 ? -5.876  6.055   13.047  0.50 20.60 ? 240  SER A CB    1 
ATOM   1762 O OG    A SER A 1 240 ? -4.905  5.664   13.329  0.50 16.87 ? 240  SER A OG    1 
ATOM   1763 O OG    B SER A 1 240 ? -6.416  7.224   13.644  0.50 26.40 ? 240  SER A OG    1 
ATOM   1764 N N     . LEU A 1 241 ? -5.891  3.528   11.196  1.00 18.01 ? 241  LEU A N     1 
ATOM   1765 C CA    . LEU A 1 241 ? -5.503  2.897   9.946   1.00 18.01 ? 241  LEU A CA    1 
ATOM   1766 C C     . LEU A 1 241 ? -6.739  2.309   9.272   1.00 15.60 ? 241  LEU A C     1 
ATOM   1767 O O     . LEU A 1 241 ? -6.894  2.429   8.062   1.00 18.90 ? 241  LEU A O     1 
ATOM   1768 C CB    . LEU A 1 241 ? -4.467  1.843   10.308  1.00 18.54 ? 241  LEU A CB    1 
ATOM   1769 C CG    . LEU A 1 241 ? -3.688  1.212   9.166   1.00 22.50 ? 241  LEU A CG    1 
ATOM   1770 C CD1   . LEU A 1 241 ? -2.953  2.267   8.339   1.00 22.94 ? 241  LEU A CD1   1 
ATOM   1771 C CD2   . LEU A 1 241 ? -2.735  0.211   9.788   1.00 22.52 ? 241  LEU A CD2   1 
ATOM   1772 N N     . LEU A 1 242 ? -7.694  1.765   10.040  1.00 14.24 ? 242  LEU A N     1 
ATOM   1773 C CA    . LEU A 1 242 ? -8.923  1.261   9.446   1.00 15.39 ? 242  LEU A CA    1 
ATOM   1774 C C     . LEU A 1 242 ? -9.752  2.409   8.868   1.00 16.80 ? 242  LEU A C     1 
ATOM   1775 O O     . LEU A 1 242 ? -10.249 2.335   7.739   1.00 18.24 ? 242  LEU A O     1 
ATOM   1776 C CB    . LEU A 1 242 ? -9.723  0.488   10.494  1.00 15.29 ? 242  LEU A CB    1 
ATOM   1777 C CG    . LEU A 1 242 ? -11.082 -0.066  10.052  1.00 14.89 ? 242  LEU A CG    1 
ATOM   1778 C CD1   . LEU A 1 242 ? -10.986 -1.029  8.898   1.00 15.19 ? 242  LEU A CD1   1 
ATOM   1779 C CD2   . LEU A 1 242 ? -11.703 -0.764  11.264  1.00 14.53 ? 242  LEU A CD2   1 
ATOM   1780 N N     . ALA A 1 243 ? -9.859  3.502   9.632   1.00 16.92 ? 243  ALA A N     1 
ATOM   1781 C CA    . ALA A 1 243 ? -10.719 4.612   9.279   1.00 17.55 ? 243  ALA A CA    1 
ATOM   1782 C C     . ALA A 1 243 ? -10.160 5.374   8.078   1.00 18.31 ? 243  ALA A C     1 
ATOM   1783 O O     . ALA A 1 243 ? -10.928 6.035   7.381   1.00 21.65 ? 243  ALA A O     1 
ATOM   1784 C CB    . ALA A 1 243 ? -10.867 5.538   10.477  1.00 17.86 ? 243  ALA A CB    1 
ATOM   1785 N N     . GLY A 1 244 ? -8.855  5.309   7.863   1.00 17.00 ? 244  GLY A N     1 
ATOM   1786 C CA    . GLY A 1 244 ? -8.197  6.110   6.832   1.00 20.13 ? 244  GLY A CA    1 
ATOM   1787 C C     . GLY A 1 244 ? -8.511  5.621   5.420   1.00 22.33 ? 244  GLY A C     1 
ATOM   1788 O O     . GLY A 1 244 ? -8.276  6.362   4.463   1.00 21.57 ? 244  GLY A O     1 
ATOM   1789 N N     . GLY A 1 245 ? -8.904  4.335   5.306   1.00 20.82 ? 245  GLY A N     1 
ATOM   1790 C CA    . GLY A 1 245 ? -9.263  3.693   4.046   1.00 22.01 ? 245  GLY A CA    1 
ATOM   1791 C C     . GLY A 1 245 ? -8.082  3.189   3.214   1.00 21.56 ? 245  GLY A C     1 
ATOM   1792 O O     . GLY A 1 245 ? -8.301  2.748   2.085   1.00 23.60 ? 245  GLY A O     1 
ATOM   1793 N N     . SER A 1 246 ? -6.843  3.196   3.743   1.00 20.35 ? 246  SER A N     1 
ATOM   1794 C CA    . SER A 1 246 ? -5.715  2.713   2.969   1.00 21.02 ? 246  SER A CA    1 
ATOM   1795 C C     . SER A 1 246 ? -5.588  1.192   2.996   1.00 19.52 ? 246  SER A C     1 
ATOM   1796 O O     . SER A 1 246 ? -4.793  0.655   2.243   1.00 19.59 ? 246  SER A O     1 
ATOM   1797 C CB    . SER A 1 246 ? -4.401  3.325   3.382   1.00 23.91 ? 246  SER A CB    1 
ATOM   1798 O OG    . SER A 1 246 ? -3.962  2.879   4.659   1.00 21.87 ? 246  SER A OG    1 
ATOM   1799 N N     . LEU A 1 247 ? -6.271  0.508   3.924   1.00 19.18 ? 247  LEU A N     1 
ATOM   1800 C CA    . LEU A 1 247 ? -6.104  -0.930  4.004   1.00 18.57 ? 247  LEU A CA    1 
ATOM   1801 C C     . LEU A 1 247 ? -6.675  -1.564  2.744   1.00 17.97 ? 247  LEU A C     1 
ATOM   1802 O O     . LEU A 1 247 ? -7.734  -1.158  2.264   1.00 17.84 ? 247  LEU A O     1 
ATOM   1803 C CB    . LEU A 1 247 ? -6.815  -1.478  5.247   1.00 18.85 ? 247  LEU A CB    1 
ATOM   1804 C CG    . LEU A 1 247 ? -6.200  -1.093  6.601   1.00 21.35 ? 247  LEU A CG    1 
ATOM   1805 C CD1   . LEU A 1 247 ? -7.116  -1.687  7.647   1.00 21.88 ? 247  LEU A CD1   1 
ATOM   1806 C CD2   . LEU A 1 247 ? -4.759  -1.578  6.766   1.00 22.28 ? 247  LEU A CD2   1 
ATOM   1807 N N     . PRO A 1 248 ? -6.089  -2.672  2.254   1.00 18.64 ? 248  PRO A N     1 
ATOM   1808 C CA    . PRO A 1 248 ? -6.691  -3.404  1.137   1.00 19.27 ? 248  PRO A CA    1 
ATOM   1809 C C     . PRO A 1 248 ? -8.102  -3.836  1.515   1.00 19.76 ? 248  PRO A C     1 
ATOM   1810 O O     . PRO A 1 248 ? -8.329  -4.367  2.600   1.00 16.88 ? 248  PRO A O     1 
ATOM   1811 C CB    . PRO A 1 248 ? -5.787  -4.597  0.875   1.00 20.28 ? 248  PRO A CB    1 
ATOM   1812 C CG    . PRO A 1 248 ? -4.487  -4.245  1.580   1.00 21.88 ? 248  PRO A CG    1 
ATOM   1813 C CD    . PRO A 1 248 ? -4.825  -3.260  2.710   1.00 19.41 ? 248  PRO A CD    1 
ATOM   1814 N N     . GLN A 1 249 ? -9.038  -3.649  0.583   1.00 20.03 ? 249  GLN A N     1 
ATOM   1815 C CA    . GLN A 1 249 ? -10.439 -3.981  0.814   1.00 22.34 ? 249  GLN A CA    1 
ATOM   1816 C C     . GLN A 1 249 ? -10.635 -5.448  1.168   1.00 18.64 ? 249  GLN A C     1 
ATOM   1817 O O     . GLN A 1 249 ? -11.599 -5.784  1.873   1.00 22.72 ? 249  GLN A O     1 
ATOM   1818 C CB    . GLN A 1 249 ? -11.304 -3.758  -0.431  1.00 23.79 ? 249  GLN A CB    1 
ATOM   1819 C CG    . GLN A 1 249 ? -11.453 -2.283  -0.769  1.00 29.64 ? 249  GLN A CG    1 
ATOM   1820 C CD    . GLN A 1 249 ? -12.137 -1.530  0.345   1.00 38.51 ? 249  GLN A CD    1 
ATOM   1821 O OE1   . GLN A 1 249 ? -11.493 -0.884  1.186   1.00 51.23 ? 249  GLN A OE1   1 
ATOM   1822 N NE2   . GLN A 1 249 ? -13.455 -1.649  0.374   1.00 36.55 ? 249  GLN A NE2   1 
ATOM   1823 N N     . HIS A 1 250 ? -9.805  -6.328  0.621   1.00 17.13 ? 250  HIS A N     1 
ATOM   1824 C CA    . HIS A 1 250 ? -10.041 -7.755  0.747   1.00 18.72 ? 250  HIS A CA    1 
ATOM   1825 C C     . HIS A 1 250 ? -9.489  -8.365  2.042   1.00 16.86 ? 250  HIS A C     1 
ATOM   1826 O O     . HIS A 1 250 ? -9.719  -9.538  2.303   1.00 18.45 ? 250  HIS A O     1 
ATOM   1827 C CB    . HIS A 1 250 ? -9.402  -8.521  -0.413  1.00 19.08 ? 250  HIS A CB    1 
ATOM   1828 C CG    . HIS A 1 250 ? -10.072 -8.336  -1.725  1.00 20.90 ? 250  HIS A CG    1 
ATOM   1829 N ND1   . HIS A 1 250 ? -11.159 -7.510  -1.942  1.00 23.99 ? 250  HIS A ND1   1 
ATOM   1830 C CD2   . HIS A 1 250 ? -9.796  -8.929  -2.889  1.00 22.29 ? 250  HIS A CD2   1 
ATOM   1831 C CE1   . HIS A 1 250 ? -11.500 -7.583  -3.231  1.00 23.84 ? 250  HIS A CE1   1 
ATOM   1832 N NE2   . HIS A 1 250 ? -10.692 -8.436  -3.810  1.00 26.99 ? 250  HIS A NE2   1 
ATOM   1833 N N     . MET A 1 251 ? -8.735  -7.591  2.828   1.00 15.94 ? 251  MET A N     1 
ATOM   1834 C CA    . MET A 1 251 ? -7.932  -8.141  3.901   1.00 15.08 ? 251  MET A CA    1 
ATOM   1835 C C     . MET A 1 251 ? -8.741  -8.156  5.201   1.00 14.41 ? 251  MET A C     1 
ATOM   1836 O O     . MET A 1 251 ? -9.254  -7.116  5.590   1.00 16.39 ? 251  MET A O     1 
ATOM   1837 C CB    . MET A 1 251 ? -6.705  -7.252  4.097   1.00 17.24 ? 251  MET A CB    1 
ATOM   1838 C CG    . MET A 1 251 ? -5.694  -7.821  5.054   1.00 20.27 ? 251  MET A CG    1 
ATOM   1839 S SD    . MET A 1 251 ? -4.271  -6.724  5.185   1.00 22.66 ? 251  MET A SD    1 
ATOM   1840 C CE    . MET A 1 251 ? -4.937  -5.448  6.251   1.00 23.20 ? 251  MET A CE    1 
ATOM   1841 N N     . ALA A 1 252 ? -8.752  -9.291  5.918   1.00 13.25 ? 252  ALA A N     1 
ATOM   1842 C CA    . ALA A 1 252 ? -9.338  -9.360  7.244   1.00 12.50 ? 252  ALA A CA    1 
ATOM   1843 C C     . ALA A 1 252 ? -8.387  -8.680  8.237   1.00 12.76 ? 252  ALA A C     1 
ATOM   1844 O O     . ALA A 1 252 ? -7.182  -8.844  8.092   1.00 14.97 ? 252  ALA A O     1 
ATOM   1845 C CB    . ALA A 1 252 ? -9.582  -10.813 7.660   1.00 13.53 ? 252  ALA A CB    1 
ATOM   1846 N N     . TYR A 1 253 ? -8.937  -7.981  9.238   1.00 12.12 ? 253  TYR A N     1 
ATOM   1847 C CA    . TYR A 1 253 ? -8.139  -7.123  10.104  1.00 13.22 ? 253  TYR A CA    1 
ATOM   1848 C C     . TYR A 1 253 ? -8.810  -6.998  11.460  1.00 13.85 ? 253  TYR A C     1 
ATOM   1849 O O     . TYR A 1 253 ? -9.938  -6.522  11.540  1.00 14.97 ? 253  TYR A O     1 
ATOM   1850 C CB    . TYR A 1 253 ? -8.094  -5.748  9.436   1.00 13.39 ? 253  TYR A CB    1 
ATOM   1851 C CG    . TYR A 1 253 ? -7.343  -4.602  10.103  1.00 12.62 ? 253  TYR A CG    1 
ATOM   1852 C CD1   . TYR A 1 253 ? -5.959  -4.495  10.031  1.00 13.41 ? 253  TYR A CD1   1 
ATOM   1853 C CD2   . TYR A 1 253 ? -8.038  -3.571  10.726  1.00 13.97 ? 253  TYR A CD2   1 
ATOM   1854 C CE1   . TYR A 1 253 ? -5.299  -3.389  10.557  1.00 13.20 ? 253  TYR A CE1   1 
ATOM   1855 C CE2   . TYR A 1 253 ? -7.383  -2.489  11.291  1.00 13.94 ? 253  TYR A CE2   1 
ATOM   1856 C CZ    . TYR A 1 253 ? -6.008  -2.378  11.182  1.00 13.23 ? 253  TYR A CZ    1 
ATOM   1857 O OH    . TYR A 1 253 ? -5.423  -1.246  11.699  1.00 14.74 ? 253  TYR A OH    1 
ATOM   1858 N N     . ASP A 1 254 ? -8.150  -7.526  12.485  1.00 14.98 ? 254  ASP A N     1 
ATOM   1859 C CA    . ASP A 1 254 ? -8.720  -7.619  13.812  1.00 14.61 ? 254  ASP A CA    1 
ATOM   1860 C C     . ASP A 1 254 ? -7.628  -7.285  14.836  1.00 14.67 ? 254  ASP A C     1 
ATOM   1861 O O     . ASP A 1 254 ? -6.426  -7.351  14.536  1.00 13.66 ? 254  ASP A O     1 
ATOM   1862 C CB    . ASP A 1 254 ? -9.132  -9.041  14.171  1.00 18.49 ? 254  ASP A CB    1 
ATOM   1863 C CG    . ASP A 1 254 ? -9.962  -9.796  13.151  1.00 29.55 ? 254  ASP A CG    1 
ATOM   1864 O OD1   . ASP A 1 254 ? -11.127 -9.367  12.897  1.00 36.49 ? 254  ASP A OD1   1 
ATOM   1865 O OD2   . ASP A 1 254 ? -9.414  -10.782 12.577  1.00 39.64 ? 254  ASP A OD2   1 
ATOM   1866 N N     . LEU A 1 255 ? -8.068  -6.881  16.027  1.00 12.82 ? 255  LEU A N     1 
ATOM   1867 C CA    . LEU A 1 255 ? -7.175  -6.582  17.147  1.00 12.77 ? 255  LEU A CA    1 
ATOM   1868 C C     . LEU A 1 255 ? -7.768  -7.258  18.366  1.00 12.66 ? 255  LEU A C     1 
ATOM   1869 O O     . LEU A 1 255 ? -8.913  -6.967  18.687  1.00 13.13 ? 255  LEU A O     1 
ATOM   1870 C CB    . LEU A 1 255 ? -7.107  -5.089  17.419  1.00 13.19 ? 255  LEU A CB    1 
ATOM   1871 C CG    . LEU A 1 255 ? -6.102  -4.642  18.492  1.00 14.35 ? 255  LEU A CG    1 
ATOM   1872 C CD1   . LEU A 1 255 ? -4.689  -4.932  18.072  1.00 13.92 ? 255  LEU A CD1   1 
ATOM   1873 C CD2   . LEU A 1 255 ? -6.234  -3.148  18.707  1.00 15.53 ? 255  LEU A CD2   1 
ATOM   1874 N N     . VAL A 1 256 ? -6.985  -8.049  19.105  1.00 11.75 ? 256  VAL A N     1 
ATOM   1875 C CA    . VAL A 1 256 ? -7.509  -8.696  20.295  1.00 11.77 ? 256  VAL A CA    1 
ATOM   1876 C C     . VAL A 1 256 ? -6.687  -8.223  21.495  1.00 12.29 ? 256  VAL A C     1 
ATOM   1877 O O     . VAL A 1 256 ? -5.479  -8.385  21.476  1.00 12.62 ? 256  VAL A O     1 
ATOM   1878 C CB    . VAL A 1 256 ? -7.458  -10.227 20.203  1.00 13.49 ? 256  VAL A CB    1 
ATOM   1879 C CG1   . VAL A 1 256 ? -7.973  -10.857 21.486  1.00 14.48 ? 256  VAL A CG1   1 
ATOM   1880 C CG2   . VAL A 1 256 ? -8.275  -10.729 19.019  1.00 13.33 ? 256  VAL A CG2   1 
ATOM   1881 N N     . ALA A 1 257 ? -7.363  -7.684  22.519  1.00 12.32 ? 257  ALA A N     1 
ATOM   1882 C CA    . ALA A 1 257 ? -6.702  -7.353  23.768  1.00 11.98 ? 257  ALA A CA    1 
ATOM   1883 C C     . ALA A 1 257 ? -6.958  -8.475  24.758  1.00 13.33 ? 257  ALA A C     1 
ATOM   1884 O O     . ALA A 1 257 ? -8.118  -8.817  25.023  1.00 12.55 ? 257  ALA A O     1 
ATOM   1885 C CB    . ALA A 1 257 ? -7.169  -6.020  24.293  1.00 12.47 ? 257  ALA A CB    1 
ATOM   1886 N N     . THR A 1 258 ? -5.880  -8.943  25.389  1.00 13.17 ? 258  THR A N     1 
ATOM   1887 C CA    . THR A 1 258 ? -5.977  -9.852  26.527  1.00 14.41 ? 258  THR A CA    1 
ATOM   1888 C C     . THR A 1 258 ? -5.238  -9.213  27.696  1.00 15.42 ? 258  THR A C     1 
ATOM   1889 O O     . THR A 1 258 ? -4.791  -8.067  27.614  1.00 14.98 ? 258  THR A O     1 
ATOM   1890 C CB    . THR A 1 258 ? -5.392  -11.220 26.205  1.00 16.83 ? 258  THR A CB    1 
ATOM   1891 O OG1   . THR A 1 258 ? -4.005  -11.074 25.907  1.00 18.83 ? 258  THR A OG1   1 
ATOM   1892 C CG2   . THR A 1 258 ? -6.112  -11.915 25.072  1.00 19.38 ? 258  THR A CG2   1 
ATOM   1893 N N     . ALA A 1 259 ? -5.086  -9.965  28.791  1.00 15.05 ? 259  ALA A N     1 
ATOM   1894 C CA    . ALA A 1 259 ? -4.553  -9.333  29.984  1.00 16.02 ? 259  ALA A CA    1 
ATOM   1895 C C     . ALA A 1 259 ? -3.104  -8.917  29.766  1.00 17.65 ? 259  ALA A C     1 
ATOM   1896 O O     . ALA A 1 259 ? -2.670  -7.925  30.342  1.00 19.86 ? 259  ALA A O     1 
ATOM   1897 C CB    . ALA A 1 259 ? -4.685  -10.243 31.178  1.00 17.28 ? 259  ALA A CB    1 
ATOM   1898 N N     . ASN A 1 260 ? -2.390  -9.655  28.910  1.00 17.04 ? 260  ASN A N     1 
ATOM   1899 C CA    . ASN A 1 260 ? -0.962  -9.494  28.771  1.00 18.61 ? 260  ASN A CA    1 
ATOM   1900 C C     . ASN A 1 260 ? -0.522  -9.276  27.327  1.00 15.60 ? 260  ASN A C     1 
ATOM   1901 O O     . ASN A 1 260 ? 0.684   -9.279  27.080  1.00 15.15 ? 260  ASN A O     1 
ATOM   1902 C CB    . ASN A 1 260 ? -0.213  -10.739 29.254  1.00 25.24 ? 260  ASN A CB    1 
ATOM   1903 C CG    . ASN A 1 260 ? -0.150  -10.800 30.755  1.00 36.31 ? 260  ASN A CG    1 
ATOM   1904 O OD1   . ASN A 1 260 ? 0.552   -9.999  31.381  1.00 45.06 ? 260  ASN A OD1   1 
ATOM   1905 N ND2   . ASN A 1 260 ? -0.889  -11.718 31.355  1.00 46.35 ? 260  ASN A ND2   1 
ATOM   1906 N N     . SER A 1 261 ? -1.455  -9.112  26.372  1.00 14.43 ? 261  SER A N     1 
ATOM   1907 C CA    . SER A 1 261 ? -1.030  -8.899  25.002  1.00 15.30 ? 261  SER A CA    1 
ATOM   1908 C C     . SER A 1 261 ? -2.088  -8.128  24.226  1.00 14.21 ? 261  SER A C     1 
ATOM   1909 O O     . SER A 1 261 ? -3.253  -8.047  24.619  1.00 12.67 ? 261  SER A O     1 
ATOM   1910 C CB    . SER A 1 261 ? -0.689  -10.211 24.300  1.00 18.44 ? 261  SER A CB    1 
ATOM   1911 O OG    . SER A 1 261 ? -1.874  -10.953 24.138  1.00 20.46 ? 261  SER A OG    1 
ATOM   1912 N N     . MET A 1 262 ? -1.611  -7.543  23.130  1.00 14.77 ? 262  MET A N     1 
ATOM   1913 C CA    . MET A 1 262 ? -2.424  -7.039  22.037  1.00 13.40 ? 262  MET A CA    1 
ATOM   1914 C C     . MET A 1 262 ? -2.002  -7.816  20.795  1.00 15.24 ? 262  MET A C     1 
ATOM   1915 O O     . MET A 1 262 ? -0.801  -7.912  20.548  1.00 14.95 ? 262  MET A O     1 
ATOM   1916 C CB    . MET A 1 262 ? -2.174  -5.544  21.790  1.00 14.23 ? 262  MET A CB    1 
ATOM   1917 C CG    . MET A 1 262 ? -2.373  -4.663  23.022  1.00 14.60 ? 262  MET A CG    1 
ATOM   1918 S SD    . MET A 1 262 ? -4.099  -4.541  23.515  1.00 15.25 ? 262  MET A SD    1 
ATOM   1919 C CE    . MET A 1 262 ? -4.636  -3.427  22.218  1.00 16.43 ? 262  MET A CE    1 
ATOM   1920 N N     . ILE A 1 263 ? -2.980  -8.383  20.055  1.00 15.17 ? 263  ILE A N     1 
ATOM   1921 C CA    . ILE A 1 263 ? -2.682  -9.184  18.875  1.00 15.53 ? 263  ILE A CA    1 
ATOM   1922 C C     . ILE A 1 263 ? -3.425  -8.616  17.672  1.00 14.72 ? 263  ILE A C     1 
ATOM   1923 O O     . ILE A 1 263 ? -4.650  -8.608  17.647  1.00 13.92 ? 263  ILE A O     1 
ATOM   1924 C CB    . ILE A 1 263 ? -2.986  -10.670 19.072  1.00 18.26 ? 263  ILE A CB    1 
ATOM   1925 C CG1   . ILE A 1 263 ? -2.288  -11.177 20.311  1.00 22.13 ? 263  ILE A CG1   1 
ATOM   1926 C CG2   . ILE A 1 263 ? -2.585  -11.456 17.815  1.00 19.31 ? 263  ILE A CG2   1 
ATOM   1927 C CD1   . ILE A 1 263 ? -2.007  -12.674 20.303  1.00 24.30 ? 263  ILE A CD1   1 
ATOM   1928 N N     . LEU A 1 264 ? -2.657  -8.065  16.729  1.00 15.30 ? 264  LEU A N     1 
ATOM   1929 C CA    . LEU A 1 264 ? -3.157  -7.615  15.430  1.00 16.10 ? 264  LEU A CA    1 
ATOM   1930 C C     . LEU A 1 264 ? -3.118  -8.823  14.497  1.00 15.24 ? 264  LEU A C     1 
ATOM   1931 O O     . LEU A 1 264 ? -2.055  -9.363  14.259  1.00 16.88 ? 264  LEU A O     1 
ATOM   1932 C CB    . LEU A 1 264 ? -2.293  -6.460  14.905  1.00 16.34 ? 264  LEU A CB    1 
ATOM   1933 C CG    . LEU A 1 264 ? -2.347  -6.159  13.403  1.00 19.11 ? 264  LEU A CG    1 
ATOM   1934 C CD1   . LEU A 1 264 ? -3.724  -5.812  12.947  1.00 19.95 ? 264  LEU A CD1   1 
ATOM   1935 C CD2   . LEU A 1 264 ? -1.322  -5.098  12.999  1.00 21.42 ? 264  LEU A CD2   1 
ATOM   1936 N N     . GLY A 1 265 ? -4.260  -9.247  13.976  1.00 15.75 ? 265  GLY A N     1 
ATOM   1937 C CA    . GLY A 1 265 ? -4.297  -10.473 13.193  1.00 16.76 ? 265  GLY A CA    1 
ATOM   1938 C C     . GLY A 1 265 ? -5.295  -10.354 12.054  1.00 15.66 ? 265  GLY A C     1 
ATOM   1939 O O     . GLY A 1 265 ? -6.111  -9.447  12.037  1.00 17.68 ? 265  GLY A O     1 
ATOM   1940 N N     . GLY A 1 266 ? -5.221  -11.287 11.118  1.00 15.76 ? 266  GLY A N     1 
ATOM   1941 C CA    . GLY A 1 266 ? -6.096  -11.239 9.973   1.00 15.26 ? 266  GLY A CA    1 
ATOM   1942 C C     . GLY A 1 266 ? -5.667  -12.220 8.895   1.00 15.49 ? 266  GLY A C     1 
ATOM   1943 O O     . GLY A 1 266 ? -4.880  -13.145 9.128   1.00 16.40 ? 266  GLY A O     1 
ATOM   1944 N N     . ALA A 1 267 ? -6.147  -11.941 7.690   1.00 15.39 ? 267  ALA A N     1 
ATOM   1945 C CA    . ALA A 1 267 ? -5.881  -12.792 6.551   1.00 15.93 ? 267  ALA A CA    1 
ATOM   1946 C C     . ALA A 1 267 ? -5.766  -11.894 5.340   1.00 16.73 ? 267  ALA A C     1 
ATOM   1947 O O     . ALA A 1 267 ? -6.545  -10.959 5.199   1.00 18.16 ? 267  ALA A O     1 
ATOM   1948 C CB    . ALA A 1 267 ? -7.004  -13.770 6.357   1.00 17.18 ? 267  ALA A CB    1 
ATOM   1949 N N     . TYR A 1 268 ? -4.804  -12.227 4.477   1.00 15.33 ? 268  TYR A N     1 
ATOM   1950 C CA    . TYR A 1 268 ? -4.564  -11.473 3.265   1.00 16.50 ? 268  TYR A CA    1 
ATOM   1951 C C     . TYR A 1 268 ? -4.674  -12.448 2.112   1.00 16.39 ? 268  TYR A C     1 
ATOM   1952 O O     . TYR A 1 268 ? -3.990  -13.472 2.131   1.00 17.73 ? 268  TYR A O     1 
ATOM   1953 C CB    . TYR A 1 268 ? -3.171  -10.839 3.328   1.00 18.01 ? 268  TYR A CB    1 
ATOM   1954 C CG    . TYR A 1 268 ? -2.770  -10.094 2.067   1.00 20.00 ? 268  TYR A CG    1 
ATOM   1955 C CD1   . TYR A 1 268 ? -3.145  -8.775  1.868   1.00 21.74 ? 268  TYR A CD1   1 
ATOM   1956 C CD2   . TYR A 1 268 ? -1.984  -10.718 1.100   1.00 21.19 ? 268  TYR A CD2   1 
ATOM   1957 C CE1   . TYR A 1 268 ? -2.745  -8.076  0.746   1.00 25.45 ? 268  TYR A CE1   1 
ATOM   1958 C CE2   . TYR A 1 268 ? -1.616  -10.048 -0.049  1.00 23.97 ? 268  TYR A CE2   1 
ATOM   1959 C CZ    . TYR A 1 268 ? -2.014  -8.732  -0.233  1.00 25.92 ? 268  TYR A CZ    1 
ATOM   1960 O OH    . TYR A 1 268 ? -1.610  -8.024  -1.323  1.00 27.93 ? 268  TYR A OH    1 
ATOM   1961 N N     . PHE A 1 269 ? -5.486  -12.077 1.107   1.00 17.19 ? 269  PHE A N     1 
ATOM   1962 C CA    . PHE A 1 269 ? -5.780  -12.979 0.011   1.00 17.38 ? 269  PHE A CA    1 
ATOM   1963 C C     . PHE A 1 269 ? -4.933  -12.569 -1.195  1.00 19.78 ? 269  PHE A C     1 
ATOM   1964 O O     . PHE A 1 269 ? -5.382  -11.830 -2.041  1.00 24.29 ? 269  PHE A O     1 
ATOM   1965 C CB    . PHE A 1 269 ? -7.296  -13.025 -0.201  1.00 17.38 ? 269  PHE A CB    1 
ATOM   1966 C CG    . PHE A 1 269 ? -8.007  -13.582 1.019   1.00 16.77 ? 269  PHE A CG    1 
ATOM   1967 C CD1   . PHE A 1 269 ? -7.891  -14.923 1.372   1.00 16.18 ? 269  PHE A CD1   1 
ATOM   1968 C CD2   . PHE A 1 269 ? -8.727  -12.745 1.865   1.00 19.11 ? 269  PHE A CD2   1 
ATOM   1969 C CE1   . PHE A 1 269 ? -8.519  -15.438 2.500   1.00 15.64 ? 269  PHE A CE1   1 
ATOM   1970 C CE2   . PHE A 1 269 ? -9.375  -13.264 2.969   1.00 17.30 ? 269  PHE A CE2   1 
ATOM   1971 C CZ    . PHE A 1 269 ? -9.244  -14.598 3.305   1.00 16.91 ? 269  PHE A CZ    1 
ATOM   1972 N N     . GLY A 1 270 ? -3.718  -13.090 -1.208  1.00 23.03 ? 270  GLY A N     1 
ATOM   1973 C CA    . GLY A 1 270 ? -2.670  -12.671 -2.122  1.00 23.63 ? 270  GLY A CA    1 
ATOM   1974 C C     . GLY A 1 270 ? -1.376  -13.328 -1.687  1.00 22.52 ? 270  GLY A C     1 
ATOM   1975 O O     . GLY A 1 270 ? -1.392  -14.255 -0.866  1.00 24.53 ? 270  GLY A O     1 
ATOM   1976 N N     . SER A 1 271 ? -0.258  -12.910 -2.314  1.00 24.53 ? 271  SER A N     1 
ATOM   1977 C CA    . SER A 1 271 ? 1.012   -13.543 -2.030  1.00 26.97 ? 271  SER A CA    1 
ATOM   1978 C C     . SER A 1 271 ? 1.541   -13.010 -0.703  1.00 24.70 ? 271  SER A C     1 
ATOM   1979 O O     . SER A 1 271 ? 1.277   -11.853 -0.378  1.00 27.33 ? 271  SER A O     1 
ATOM   1980 C CB    . SER A 1 271 ? 2.022   -13.297 -3.133  1.00 30.99 ? 271  SER A CB    1 
ATOM   1981 O OG    . SER A 1 271 ? 2.239   -11.902 -3.293  1.00 32.06 ? 271  SER A OG    1 
ATOM   1982 N N     . GLN A 1 272 ? 2.325   -13.849 -0.024  1.00 27.67 ? 272  GLN A N     1 
ATOM   1983 C CA    . GLN A 1 272 ? 3.028   -13.483 1.197   1.00 29.21 ? 272  GLN A CA    1 
ATOM   1984 C C     . GLN A 1 272 ? 3.947   -12.290 0.925   1.00 34.11 ? 272  GLN A C     1 
ATOM   1985 O O     . GLN A 1 272 ? 4.014   -11.360 1.719   1.00 35.25 ? 272  GLN A O     1 
ATOM   1986 C CB    . GLN A 1 272 ? 3.767   -14.688 1.757   1.00 31.01 ? 272  GLN A CB    1 
ATOM   1987 C CG    . GLN A 1 272 ? 4.261   -14.464 3.174   1.00 33.06 ? 272  GLN A CG    1 
ATOM   1988 C CD    . GLN A 1 272 ? 4.859   -15.697 3.799   1.00 35.27 ? 272  GLN A CD    1 
ATOM   1989 O OE1   . GLN A 1 272 ? 4.333   -16.811 3.690   1.00 38.69 ? 272  GLN A OE1   1 
ATOM   1990 N NE2   . GLN A 1 272 ? 5.964   -15.505 4.502   1.00 39.44 ? 272  GLN A NE2   1 
ATOM   1991 N N     . GLU A 1 273 ? 4.602   -12.307 -0.237  1.00 37.53 ? 273  GLU A N     1 
ATOM   1992 C CA    . GLU A 1 273 ? 5.511   -11.257 -0.665  1.00 37.19 ? 273  GLU A CA    1 
ATOM   1993 C C     . GLU A 1 273 ? 4.758   -9.931  -0.715  1.00 34.29 ? 273  GLU A C     1 
ATOM   1994 O O     . GLU A 1 273 ? 5.244   -8.929  -0.202  1.00 32.23 ? 273  GLU A O     1 
ATOM   1995 C CB    . GLU A 1 273 ? 6.133   -11.654 -2.012  1.00 42.22 ? 273  GLU A CB    1 
ATOM   1996 C CG    . GLU A 1 273 ? 7.074   -12.862 -1.931  1.00 48.52 ? 273  GLU A CG    1 
ATOM   1997 C CD    . GLU A 1 273 ? 6.527   -14.292 -1.929  1.00 52.53 ? 273  GLU A CD    1 
ATOM   1998 O OE1   . GLU A 1 273 ? 5.322   -14.566 -2.190  1.00 48.38 ? 273  GLU A OE1   1 
ATOM   1999 O OE2   . GLU A 1 273 ? 7.371   -15.175 -1.624  1.00 53.09 ? 273  GLU A OE2   1 
ATOM   2000 N N     . ASP A 1 274 ? 3.580   -9.926  -1.339  1.00 29.64 ? 274  ASP A N     1 
ATOM   2001 C CA    . ASP A 1 274 ? 2.802   -8.707  -1.447  1.00 28.35 ? 274  ASP A CA    1 
ATOM   2002 C C     . ASP A 1 274 ? 2.300   -8.274  -0.064  1.00 30.18 ? 274  ASP A C     1 
ATOM   2003 O O     . ASP A 1 274 ? 2.156   -7.086  0.192   1.00 28.38 ? 274  ASP A O     1 
ATOM   2004 C CB    . ASP A 1 274 ? 1.654   -8.843  -2.424  1.00 32.64 ? 274  ASP A CB    1 
ATOM   2005 C CG    . ASP A 1 274 ? 2.030   -8.926  -3.902  1.00 35.86 ? 274  ASP A CG    1 
ATOM   2006 O OD1   . ASP A 1 274 ? 3.219   -8.738  -4.231  1.00 34.74 ? 274  ASP A OD1   1 
ATOM   2007 O OD2   . ASP A 1 274 ? 1.132   -9.208  -4.711  1.00 36.17 ? 274  ASP A OD2   1 
ATOM   2008 N N     . PHE A 1 275 ? 2.008   -9.234  0.822   1.00 30.01 ? 275  PHE A N     1 
ATOM   2009 C CA    . PHE A 1 275 ? 1.561   -8.875  2.158   1.00 26.71 ? 275  PHE A CA    1 
ATOM   2010 C C     . PHE A 1 275 ? 2.705   -8.183  2.910   1.00 29.75 ? 275  PHE A C     1 
ATOM   2011 O O     . PHE A 1 275 ? 2.517   -7.103  3.478   1.00 30.75 ? 275  PHE A O     1 
ATOM   2012 C CB    . PHE A 1 275 ? 1.038   -10.074 2.949   1.00 25.07 ? 275  PHE A CB    1 
ATOM   2013 C CG    . PHE A 1 275 ? 0.723   -9.646  4.377   1.00 21.56 ? 275  PHE A CG    1 
ATOM   2014 C CD1   . PHE A 1 275 ? -0.380  -8.848  4.655   1.00 20.96 ? 275  PHE A CD1   1 
ATOM   2015 C CD2   . PHE A 1 275 ? 1.548   -10.026 5.429   1.00 21.06 ? 275  PHE A CD2   1 
ATOM   2016 C CE1   . PHE A 1 275 ? -0.626  -8.398  5.946   1.00 17.93 ? 275  PHE A CE1   1 
ATOM   2017 C CE2   . PHE A 1 275 ? 1.297   -9.600  6.720   1.00 21.41 ? 275  PHE A CE2   1 
ATOM   2018 C CZ    . PHE A 1 275 ? 0.209   -8.795  6.981   1.00 22.33 ? 275  PHE A CZ    1 
ATOM   2019 N N     . GLU A 1 276 ? 3.868   -8.852  2.910   1.00 30.87 ? 276  GLU A N     1 
ATOM   2020 C CA    . GLU A 1 276 ? 5.067   -8.389  3.593   1.00 34.48 ? 276  GLU A CA    1 
ATOM   2021 C C     . GLU A 1 276 ? 5.450   -7.019  3.049   1.00 33.80 ? 276  GLU A C     1 
ATOM   2022 O O     . GLU A 1 276 ? 5.857   -6.143  3.804   1.00 40.62 ? 276  GLU A O     1 
ATOM   2023 C CB    . GLU A 1 276 ? 6.151   -9.462  3.519   1.00 33.80 ? 276  GLU A CB    1 
ATOM   2024 C CG    . GLU A 1 276 ? 5.962   -10.544 4.580   1.00 37.05 ? 276  GLU A CG    1 
ATOM   2025 C CD    . GLU A 1 276 ? 6.899   -11.738 4.502   1.00 40.59 ? 276  GLU A CD    1 
ATOM   2026 O OE1   . GLU A 1 276 ? 6.880   -12.576 5.426   1.00 43.01 ? 276  GLU A OE1   1 
ATOM   2027 O OE2   . GLU A 1 276 ? 7.628   -11.864 3.500   1.00 47.89 ? 276  GLU A OE2   1 
ATOM   2028 N N     . ALA A 1 277 ? 5.269   -6.830  1.751   1.00 35.21 ? 277  ALA A N     1 
ATOM   2029 C CA    . ALA A 1 277 ? 5.609   -5.574  1.110   1.00 39.00 ? 277  ALA A CA    1 
ATOM   2030 C C     . ALA A 1 277 ? 4.758   -4.442  1.671   1.00 38.94 ? 277  ALA A C     1 
ATOM   2031 O O     . ALA A 1 277 ? 5.242   -3.319  1.790   1.00 33.87 ? 277  ALA A O     1 
ATOM   2032 C CB    . ALA A 1 277 ? 5.434   -5.692  -0.386  1.00 41.00 ? 277  ALA A CB    1 
ATOM   2033 N N     . PHE A 1 278 ? 3.490   -4.735  2.003   1.00 36.99 ? 278  PHE A N     1 
ATOM   2034 C CA    . PHE A 1 278 ? 2.578   -3.735  2.536   1.00 34.53 ? 278  PHE A CA    1 
ATOM   2035 C C     . PHE A 1 278 ? 3.053   -3.267  3.918   1.00 29.37 ? 278  PHE A C     1 
ATOM   2036 O O     . PHE A 1 278 ? 2.744   -2.154  4.302   1.00 32.24 ? 278  PHE A O     1 
ATOM   2037 C CB    . PHE A 1 278 ? 1.132   -4.261  2.588   1.00 38.91 ? 278  PHE A CB    1 
ATOM   2038 C CG    . PHE A 1 278 ? 0.098   -3.263  3.084   1.00 39.22 ? 278  PHE A CG    1 
ATOM   2039 C CD1   . PHE A 1 278 ? -0.376  -2.255  2.254   1.00 41.63 ? 278  PHE A CD1   1 
ATOM   2040 C CD2   . PHE A 1 278 ? -0.422  -3.339  4.375   1.00 45.49 ? 278  PHE A CD2   1 
ATOM   2041 C CE1   . PHE A 1 278 ? -1.308  -1.335  2.703   1.00 41.62 ? 278  PHE A CE1   1 
ATOM   2042 C CE2   . PHE A 1 278 ? -1.353  -2.404  4.825   1.00 42.61 ? 278  PHE A CE2   1 
ATOM   2043 C CZ    . PHE A 1 278 ? -1.793  -1.404  3.991   1.00 44.84 ? 278  PHE A CZ    1 
ATOM   2044 N N     . ASN A 1 279 ? 3.764   -4.124  4.667   1.00 31.52 ? 279  ASN A N     1 
ATOM   2045 C CA    . ASN A 1 279 ? 4.453   -3.739  5.901   1.00 31.92 ? 279  ASN A CA    1 
ATOM   2046 C C     . ASN A 1 279 ? 3.480   -3.106  6.905   1.00 31.09 ? 279  ASN A C     1 
ATOM   2047 O O     . ASN A 1 279 ? 3.672   -1.991  7.408   1.00 28.23 ? 279  ASN A O     1 
ATOM   2048 C CB    . ASN A 1 279 ? 5.632   -2.826  5.599   1.00 33.62 ? 279  ASN A CB    1 
ATOM   2049 C CG    . ASN A 1 279 ? 6.711   -2.845  6.650   1.00 35.84 ? 279  ASN A CG    1 
ATOM   2050 O OD1   . ASN A 1 279 ? 6.690   -3.634  7.608   1.00 35.48 ? 279  ASN A OD1   1 
ATOM   2051 N ND2   . ASN A 1 279 ? 7.680   -1.962  6.467   1.00 46.22 ? 279  ASN A ND2   1 
ATOM   2052 N N     . LEU A 1 280 ? 2.462   -3.891  7.264   1.00 27.38 ? 280  LEU A N     1 
ATOM   2053 C CA    . LEU A 1 280 ? 1.370   -3.416  8.083   1.00 24.88 ? 280  LEU A CA    1 
ATOM   2054 C C     . LEU A 1 280 ? 1.874   -2.879  9.420   1.00 23.51 ? 280  LEU A C     1 
ATOM   2055 O O     . LEU A 1 280 ? 1.354   -1.863  9.884   1.00 22.37 ? 280  LEU A O     1 
ATOM   2056 C CB    . LEU A 1 280 ? 0.401   -4.588  8.247   1.00 24.83 ? 280  LEU A CB    1 
ATOM   2057 C CG    . LEU A 1 280 ? -0.874  -4.278  9.029   1.00 25.22 ? 280  LEU A CG    1 
ATOM   2058 C CD1   . LEU A 1 280 ? -1.656  -3.159  8.374   1.00 27.32 ? 280  LEU A CD1   1 
ATOM   2059 C CD2   . LEU A 1 280 ? -1.741  -5.538  9.138   1.00 23.32 ? 280  LEU A CD2   1 
ATOM   2060 N N     . SER A 1 281 ? 2.862   -3.557  10.043  1.00 23.61 ? 281  SER A N     1 
ATOM   2061 C CA    . SER A 1 281 ? 3.265   -3.226  11.405  1.00 26.35 ? 281  SER A CA    1 
ATOM   2062 C C     . SER A 1 281 ? 4.097   -1.950  11.467  1.00 23.55 ? 281  SER A C     1 
ATOM   2063 O O     . SER A 1 281 ? 4.207   -1.348  12.540  1.00 24.99 ? 281  SER A O     1 
ATOM   2064 C CB    . SER A 1 281 ? 3.978   -4.366  12.103  1.00 31.82 ? 281  SER A CB    1 
ATOM   2065 O OG    . SER A 1 281 ? 5.311   -4.541  11.645  1.00 32.16 ? 281  SER A OG    1 
ATOM   2066 N N     . SER A 1 282 ? 4.565   -1.469  10.315  1.00 24.08 ? 282  SER A N     1 
ATOM   2067 C CA    . SER A 1 282 ? 5.356   -0.247  10.255  1.00 26.25 ? 282  SER A CA    1 
ATOM   2068 C C     . SER A 1 282 ? 4.530   0.969   10.684  1.00 25.83 ? 282  SER A C     1 
ATOM   2069 O O     . SER A 1 282 ? 5.087   1.981   11.099  1.00 25.41 ? 282  SER A O     1 
ATOM   2070 C CB    . SER A 1 282 ? 5.916   -0.037  8.853   1.00 26.82 ? 282  SER A CB    1 
ATOM   2071 O OG    . SER A 1 282 ? 4.888   0.438   7.992   1.00 28.69 ? 282  SER A OG    1 
ATOM   2072 N N     . HIS A 1 283 ? 3.190   0.890   10.590  1.00 24.21 ? 283  HIS A N     1 
ATOM   2073 C CA    . HIS A 1 283 ? 2.355   2.023   10.956  1.00 24.96 ? 283  HIS A CA    1 
ATOM   2074 C C     . HIS A 1 283 ? 2.307   2.233   12.468  1.00 24.59 ? 283  HIS A C     1 
ATOM   2075 O O     . HIS A 1 283 ? 1.818   3.258   12.944  1.00 27.29 ? 283  HIS A O     1 
ATOM   2076 C CB    . HIS A 1 283 ? 0.931   1.813   10.441  1.00 31.76 ? 283  HIS A CB    1 
ATOM   2077 C CG    . HIS A 1 283 ? 0.846   1.755   8.958   1.00 34.45 ? 283  HIS A CG    1 
ATOM   2078 N ND1   . HIS A 1 283 ? 0.701   2.892   8.195   1.00 34.18 ? 283  HIS A ND1   1 
ATOM   2079 C CD2   . HIS A 1 283 ? 0.905   0.733   8.101   1.00 34.37 ? 283  HIS A CD2   1 
ATOM   2080 C CE1   . HIS A 1 283 ? 0.647   2.549   6.921   1.00 35.02 ? 283  HIS A CE1   1 
ATOM   2081 N NE2   . HIS A 1 283 ? 0.783   1.247   6.835   1.00 36.64 ? 283  HIS A NE2   1 
ATOM   2082 N N     . PHE A 1 284 ? 2.783   1.254   13.238  1.00 24.38 ? 284  PHE A N     1 
ATOM   2083 C CA    . PHE A 1 284 ? 2.732   1.365   14.686  1.00 23.40 ? 284  PHE A CA    1 
ATOM   2084 C C     . PHE A 1 284 ? 4.012   1.986   15.241  1.00 28.50 ? 284  PHE A C     1 
ATOM   2085 O O     . PHE A 1 284 ? 5.111   1.645   14.812  1.00 29.80 ? 284  PHE A O     1 
ATOM   2086 C CB    . PHE A 1 284 ? 2.445   -0.023  15.266  1.00 21.14 ? 284  PHE A CB    1 
ATOM   2087 C CG    . PHE A 1 284 ? 1.064   -0.525  14.892  1.00 20.43 ? 284  PHE A CG    1 
ATOM   2088 C CD1   . PHE A 1 284 ? 0.815   -1.078  13.647  1.00 20.63 ? 284  PHE A CD1   1 
ATOM   2089 C CD2   . PHE A 1 284 ? 0.006   -0.421  15.776  1.00 20.85 ? 284  PHE A CD2   1 
ATOM   2090 C CE1   . PHE A 1 284 ? -0.453  -1.514  13.308  1.00 19.66 ? 284  PHE A CE1   1 
ATOM   2091 C CE2   . PHE A 1 284 ? -1.262  -0.832  15.418  1.00 19.64 ? 284  PHE A CE2   1 
ATOM   2092 C CZ    . PHE A 1 284 ? -1.480  -1.404  14.204  1.00 19.80 ? 284  PHE A CZ    1 
ATOM   2093 N N     . LYS A 1 285 ? 3.828   2.898   16.197  1.00 28.94 ? 285  LYS A N     1 
ATOM   2094 C CA    . LYS A 1 285 ? 4.903   3.601   16.878  1.00 34.14 ? 285  LYS A CA    1 
ATOM   2095 C C     . LYS A 1 285 ? 5.883   2.612   17.491  1.00 30.49 ? 285  LYS A C     1 
ATOM   2096 O O     . LYS A 1 285 ? 7.094   2.743   17.345  1.00 31.03 ? 285  LYS A O     1 
ATOM   2097 C CB    . LYS A 1 285 ? 4.239   4.497   17.927  1.00 42.54 ? 285  LYS A CB    1 
ATOM   2098 C CG    . LYS A 1 285 ? 5.177   5.237   18.859  1.00 55.09 ? 285  LYS A CG    1 
ATOM   2099 C CD    . LYS A 1 285 ? 6.177   6.134   18.142  1.00 69.03 ? 285  LYS A CD    1 
ATOM   2100 C CE    . LYS A 1 285 ? 7.088   6.867   19.082  1.00 74.87 ? 285  LYS A CE    1 
ATOM   2101 N NZ    . LYS A 1 285 ? 7.940   7.801   18.339  1.00 74.47 ? 285  LYS A NZ    1 
ATOM   2102 N N     . VAL A 1 286 ? 5.357   1.599   18.179  1.00 27.25 ? 286  VAL A N     1 
ATOM   2103 C CA    . VAL A 1 286 ? 6.180   0.587   18.807  1.00 26.96 ? 286  VAL A CA    1 
ATOM   2104 C C     . VAL A 1 286 ? 6.076   -0.681  17.972  1.00 25.92 ? 286  VAL A C     1 
ATOM   2105 O O     . VAL A 1 286 ? 4.969   -1.101  17.670  1.00 23.63 ? 286  VAL A O     1 
ATOM   2106 C CB    . VAL A 1 286 ? 5.685   0.371   20.244  1.00 26.71 ? 286  VAL A CB    1 
ATOM   2107 C CG1   . VAL A 1 286 ? 6.387   -0.802  20.916  1.00 26.38 ? 286  VAL A CG1   1 
ATOM   2108 C CG2   . VAL A 1 286 ? 5.802   1.656   21.072  1.00 27.22 ? 286  VAL A CG2   1 
ATOM   2109 N N     . ALA A 1 287 ? 7.216   -1.286  17.639  1.00 26.34 ? 287  ALA A N     1 
ATOM   2110 C CA    . ALA A 1 287 ? 7.223   -2.513  16.865  1.00 25.36 ? 287  ALA A CA    1 
ATOM   2111 C C     . ALA A 1 287 ? 6.680   -3.654  17.717  1.00 26.55 ? 287  ALA A C     1 
ATOM   2112 O O     . ALA A 1 287 ? 6.944   -3.743  18.916  1.00 22.17 ? 287  ALA A O     1 
ATOM   2113 C CB    . ALA A 1 287 ? 8.603   -2.843  16.364  1.00 27.26 ? 287  ALA A CB    1 
ATOM   2114 N N     . PRO A 1 288 ? 5.893   -4.565  17.115  1.00 22.76 ? 288  PRO A N     1 
ATOM   2115 C CA    . PRO A 1 288 ? 5.422   -5.742  17.832  1.00 21.99 ? 288  PRO A CA    1 
ATOM   2116 C C     . PRO A 1 288 ? 6.622   -6.544  18.277  1.00 22.27 ? 288  PRO A C     1 
ATOM   2117 O O     . PRO A 1 288 ? 7.655   -6.538  17.616  1.00 25.90 ? 288  PRO A O     1 
ATOM   2118 C CB    . PRO A 1 288 ? 4.570   -6.541  16.834  1.00 21.66 ? 288  PRO A CB    1 
ATOM   2119 C CG    . PRO A 1 288 ? 4.800   -5.871  15.487  1.00 22.58 ? 288  PRO A CG    1 
ATOM   2120 C CD    . PRO A 1 288 ? 5.372   -4.484  15.742  1.00 22.89 ? 288  PRO A CD    1 
ATOM   2121 N N     . ASP A 1 289 ? 6.405   -7.321  19.330  1.00 20.36 ? 289  ASP A N     1 
ATOM   2122 C CA    . ASP A 1 289 ? 7.415   -8.198  19.888  1.00 20.50 ? 289  ASP A CA    1 
ATOM   2123 C C     . ASP A 1 289 ? 7.554   -9.468  19.068  1.00 24.61 ? 289  ASP A C     1 
ATOM   2124 O O     . ASP A 1 289 ? 8.618   -10.076 19.083  1.00 24.69 ? 289  ASP A O     1 
ATOM   2125 C CB    . ASP A 1 289 ? 7.091   -8.540  21.335  1.00 22.68 ? 289  ASP A CB    1 
ATOM   2126 C CG    . ASP A 1 289 ? 7.053   -7.308  22.223  1.00 25.03 ? 289  ASP A CG    1 
ATOM   2127 O OD1   . ASP A 1 289 ? 8.108   -6.643  22.378  1.00 27.99 ? 289  ASP A OD1   1 
ATOM   2128 O OD2   . ASP A 1 289 ? 5.973   -6.966  22.678  1.00 22.98 ? 289  ASP A OD2   1 
ATOM   2129 N N     . VAL A 1 290 ? 6.453   -9.906  18.446  1.00 22.20 ? 290  VAL A N     1 
ATOM   2130 C CA    . VAL A 1 290 ? 6.402   -11.177 17.731  1.00 23.63 ? 290  VAL A CA    1 
ATOM   2131 C C     . VAL A 1 290 ? 5.615   -10.948 16.439  1.00 20.00 ? 290  VAL A C     1 
ATOM   2132 O O     . VAL A 1 290 ? 4.595   -10.288 16.483  1.00 19.76 ? 290  VAL A O     1 
ATOM   2133 C CB    . VAL A 1 290 ? 5.743   -12.287 18.566  1.00 26.14 ? 290  VAL A CB    1 
ATOM   2134 C CG1   . VAL A 1 290 ? 5.657   -13.609 17.796  1.00 30.37 ? 290  VAL A CG1   1 
ATOM   2135 C CG2   . VAL A 1 290 ? 6.422   -12.502 19.915  1.00 29.53 ? 290  VAL A CG2   1 
ATOM   2136 N N     . THR A 1 291 ? 6.115   -11.455 15.300  1.00 20.74 ? 291  THR A N     1 
ATOM   2137 C CA    . THR A 1 291 ? 5.344   -11.497 14.064  1.00 22.75 ? 291  THR A CA    1 
ATOM   2138 C C     . THR A 1 291 ? 5.251   -12.947 13.590  1.00 23.71 ? 291  THR A C     1 
ATOM   2139 O O     . THR A 1 291 ? 6.238   -13.654 13.636  1.00 25.50 ? 291  THR A O     1 
ATOM   2140 C CB    . THR A 1 291 ? 5.972   -10.602 13.032  1.00 24.61 ? 291  THR A CB    1 
ATOM   2141 N N     . HIS A 1 292 ? 4.064   -13.403 13.171  1.00 23.79 ? 292  HIS A N     1 
ATOM   2142 C CA    . HIS A 1 292 ? 3.902   -14.740 12.608  1.00 26.34 ? 292  HIS A CA    1 
ATOM   2143 C C     . HIS A 1 292 ? 3.100   -14.594 11.322  1.00 26.77 ? 292  HIS A C     1 
ATOM   2144 O O     . HIS A 1 292 ? 1.952   -14.138 11.390  1.00 25.90 ? 292  HIS A O     1 
ATOM   2145 C CB    . HIS A 1 292 ? 3.062   -15.681 13.481  1.00 30.26 ? 292  HIS A CB    1 
ATOM   2146 C CG    . HIS A 1 292 ? 3.618   -16.055 14.814  1.00 36.83 ? 292  HIS A CG    1 
ATOM   2147 N ND1   . HIS A 1 292 ? 4.877   -16.576 15.023  1.00 40.69 ? 292  HIS A ND1   1 
ATOM   2148 C CD2   . HIS A 1 292 ? 3.023   -16.003 16.023  1.00 41.44 ? 292  HIS A CD2   1 
ATOM   2149 C CE1   . HIS A 1 292 ? 5.038   -16.818 16.319  1.00 40.98 ? 292  HIS A CE1   1 
ATOM   2150 N NE2   . HIS A 1 292 ? 3.924   -16.467 16.946  1.00 40.20 ? 292  HIS A NE2   1 
ATOM   2151 N N     . ILE A 1 293 ? 3.685   -15.029 10.195  1.00 22.66 ? 293  ILE A N     1 
ATOM   2152 C CA    . ILE A 1 293 ? 3.052   -14.930 8.887   1.00 24.21 ? 293  ILE A CA    1 
ATOM   2153 C C     . ILE A 1 293 ? 3.127   -16.308 8.232   1.00 25.53 ? 293  ILE A C     1 
ATOM   2154 O O     . ILE A 1 293 ? 4.175   -16.952 8.274   1.00 22.03 ? 293  ILE A O     1 
ATOM   2155 C CB    . ILE A 1 293 ? 3.741   -13.839 8.064   1.00 28.50 ? 293  ILE A CB    1 
ATOM   2156 C CG1   . ILE A 1 293 ? 3.720   -12.511 8.806   1.00 31.27 ? 293  ILE A CG1   1 
ATOM   2157 C CG2   . ILE A 1 293 ? 3.140   -13.709 6.669   1.00 28.85 ? 293  ILE A CG2   1 
ATOM   2158 C CD1   . ILE A 1 293 ? 4.596   -11.454 8.176   1.00 36.15 ? 293  ILE A CD1   1 
ATOM   2159 N N     . LYS A 1 294 ? 1.987   -16.819 7.735   1.00 22.28 ? 294  LYS A N     1 
ATOM   2160 C CA    . LYS A 1 294 ? 1.986   -18.154 7.149   1.00 22.26 ? 294  LYS A CA    1 
ATOM   2161 C C     . LYS A 1 294 ? 1.087   -18.153 5.924   1.00 25.56 ? 294  LYS A C     1 
ATOM   2162 O O     . LYS A 1 294 ? -0.014  -17.600 5.990   1.00 21.91 ? 294  LYS A O     1 
ATOM   2163 C CB    . LYS A 1 294 ? 1.512   -19.256 8.094   1.00 25.73 ? 294  LYS A CB    1 
ATOM   2164 C CG    . LYS A 1 294 ? 1.753   -20.693 7.609   1.00 26.98 ? 294  LYS A CG    1 
ATOM   2165 C CD    . LYS A 1 294 ? 1.200   -21.679 8.628   1.00 32.16 ? 294  LYS A CD    1 
ATOM   2166 C CE    . LYS A 1 294 ? 1.627   -23.095 8.503   1.00 37.65 ? 294  LYS A CE    1 
ATOM   2167 N NZ    . LYS A 1 294 ? 1.754   -23.469 7.101   1.00 44.11 ? 294  LYS A NZ    1 
ATOM   2168 N N     . THR A 1 295 ? 1.589   -18.744 4.828   1.00 22.67 ? 295  THR A N     1 
ATOM   2169 C CA    . THR A 1 295 ? 0.848   -18.854 3.578   1.00 23.55 ? 295  THR A CA    1 
ATOM   2170 C C     . THR A 1 295 ? 0.223   -20.239 3.488   1.00 22.74 ? 295  THR A C     1 
ATOM   2171 O O     . THR A 1 295 ? 0.890   -21.222 3.782   1.00 22.62 ? 295  THR A O     1 
ATOM   2172 C CB    . THR A 1 295 ? 1.758   -18.625 2.370   1.00 28.66 ? 295  THR A CB    1 
ATOM   2173 O OG1   . THR A 1 295 ? 2.133   -17.256 2.429   1.00 30.54 ? 295  THR A OG1   1 
ATOM   2174 C CG2   . THR A 1 295 ? 0.995   -18.803 1.071   1.00 30.79 ? 295  THR A CG2   1 
ATOM   2175 N N     . TYR A 1 296 ? -1.055  -20.284 3.093   1.00 21.00 ? 296  TYR A N     1 
ATOM   2176 C CA    . TYR A 1 296 ? -1.765  -21.521 2.835   1.00 20.86 ? 296  TYR A CA    1 
ATOM   2177 C C     . TYR A 1 296 ? -2.130  -21.590 1.352   1.00 20.72 ? 296  TYR A C     1 
ATOM   2178 O O     . TYR A 1 296 ? -2.851  -20.724 0.842   1.00 21.16 ? 296  TYR A O     1 
ATOM   2179 C CB    . TYR A 1 296 ? -3.055  -21.567 3.664   1.00 17.83 ? 296  TYR A CB    1 
ATOM   2180 C CG    . TYR A 1 296 ? -2.791  -21.679 5.157   1.00 18.03 ? 296  TYR A CG    1 
ATOM   2181 C CD1   . TYR A 1 296 ? -2.584  -20.542 5.933   1.00 18.30 ? 296  TYR A CD1   1 
ATOM   2182 C CD2   . TYR A 1 296 ? -2.758  -22.913 5.783   1.00 17.16 ? 296  TYR A CD2   1 
ATOM   2183 C CE1   . TYR A 1 296 ? -2.337  -20.638 7.290   1.00 16.98 ? 296  TYR A CE1   1 
ATOM   2184 C CE2   . TYR A 1 296 ? -2.507  -23.027 7.136   1.00 18.39 ? 296  TYR A CE2   1 
ATOM   2185 C CZ    . TYR A 1 296 ? -2.328  -21.883 7.898   1.00 17.88 ? 296  TYR A CZ    1 
ATOM   2186 O OH    . TYR A 1 296 ? -2.082  -21.977 9.231   1.00 19.69 ? 296  TYR A OH    1 
ATOM   2187 N N     . THR A 1 297 ? -1.620  -22.619 0.667   1.00 21.98 ? 297  THR A N     1 
ATOM   2188 C CA    . THR A 1 297 ? -2.026  -22.904 -0.698  1.00 22.50 ? 297  THR A CA    1 
ATOM   2189 C C     . THR A 1 297 ? -3.347  -23.674 -0.700  1.00 22.67 ? 297  THR A C     1 
ATOM   2190 O O     . THR A 1 297 ? -3.992  -23.732 -1.752  1.00 22.30 ? 297  THR A O     1 
ATOM   2191 C CB    . THR A 1 297 ? -0.973  -23.706 -1.480  1.00 25.21 ? 297  THR A CB    1 
ATOM   2192 O OG1   . THR A 1 297 ? -0.742  -24.932 -0.783  1.00 24.48 ? 297  THR A OG1   1 
ATOM   2193 C CG2   . THR A 1 297 ? 0.287   -22.898 -1.717  1.00 24.82 ? 297  THR A CG2   1 
ATOM   2194 N N     . ASN A 1 298 ? -3.730  -24.270 0.441   1.00 20.77 ? 298  ASN A N     1 
ATOM   2195 C CA    . ASN A 1 298 ? -4.983  -25.009 0.543   1.00 18.31 ? 298  ASN A CA    1 
ATOM   2196 C C     . ASN A 1 298 ? -5.942  -24.281 1.490   1.00 17.42 ? 298  ASN A C     1 
ATOM   2197 O O     . ASN A 1 298 ? -5.623  -24.081 2.657   1.00 16.77 ? 298  ASN A O     1 
ATOM   2198 C CB    . ASN A 1 298 ? -4.747  -26.405 1.072   1.00 18.90 ? 298  ASN A CB    1 
ATOM   2199 C CG    . ASN A 1 298 ? -6.010  -27.224 1.178   1.00 20.75 ? 298  ASN A CG    1 
ATOM   2200 O OD1   . ASN A 1 298 ? -6.858  -27.058 2.063   1.00 20.62 ? 298  ASN A OD1   1 
ATOM   2201 N ND2   . ASN A 1 298 ? -6.116  -28.211 0.324   1.00 22.56 ? 298  ASN A ND2   1 
ATOM   2202 N N     . PHE A 1 299 ? -7.115  -23.870 0.974   1.00 16.52 ? 299  PHE A N     1 
ATOM   2203 C CA    . PHE A 1 299 ? -8.022  -23.008 1.726   1.00 17.76 ? 299  PHE A CA    1 
ATOM   2204 C C     . PHE A 1 299 ? -8.687  -23.748 2.879   1.00 18.13 ? 299  PHE A C     1 
ATOM   2205 O O     . PHE A 1 299 ? -9.051  -23.103 3.857   1.00 17.18 ? 299  PHE A O     1 
ATOM   2206 C CB    . PHE A 1 299 ? -9.068  -22.405 0.771   1.00 17.97 ? 299  PHE A CB    1 
ATOM   2207 C CG    . PHE A 1 299 ? -9.957  -21.392 1.471   1.00 16.08 ? 299  PHE A CG    1 
ATOM   2208 C CD1   . PHE A 1 299 ? -9.479  -20.124 1.760   1.00 15.94 ? 299  PHE A CD1   1 
ATOM   2209 C CD2   . PHE A 1 299 ? -11.236 -21.739 1.877   1.00 15.88 ? 299  PHE A CD2   1 
ATOM   2210 C CE1   . PHE A 1 299 ? -10.262 -19.215 2.436   1.00 18.73 ? 299  PHE A CE1   1 
ATOM   2211 C CE2   . PHE A 1 299 ? -12.011 -20.835 2.542   1.00 15.65 ? 299  PHE A CE2   1 
ATOM   2212 C CZ    . PHE A 1 299 ? -11.534 -19.580 2.820   1.00 17.28 ? 299  PHE A CZ    1 
ATOM   2213 N N     . PHE A 1 300 ? -8.918  -25.065 2.737   1.00 17.24 ? 300  PHE A N     1 
ATOM   2214 C CA    . PHE A 1 300 ? -9.469  -25.881 3.803   1.00 17.41 ? 300  PHE A CA    1 
ATOM   2215 C C     . PHE A 1 300 ? -8.472  -25.860 4.970   1.00 17.98 ? 300  PHE A C     1 
ATOM   2216 O O     . PHE A 1 300 ? -8.853  -25.612 6.114   1.00 15.50 ? 300  PHE A O     1 
ATOM   2217 C CB    . PHE A 1 300 ? -9.818  -27.330 3.418   1.00 18.74 ? 300  PHE A CB    1 
ATOM   2218 C CG    . PHE A 1 300 ? -10.345 -28.090 4.620   1.00 16.93 ? 300  PHE A CG    1 
ATOM   2219 C CD1   . PHE A 1 300 ? -11.649 -27.866 5.065   1.00 17.14 ? 300  PHE A CD1   1 
ATOM   2220 C CD2   . PHE A 1 300 ? -9.523  -28.915 5.382   1.00 18.32 ? 300  PHE A CD2   1 
ATOM   2221 C CE1   . PHE A 1 300 ? -12.104 -28.469 6.218   1.00 18.58 ? 300  PHE A CE1   1 
ATOM   2222 C CE2   . PHE A 1 300 ? -9.988  -29.521 6.546   1.00 19.46 ? 300  PHE A CE2   1 
ATOM   2223 C CZ    . PHE A 1 300 ? -11.298 -29.311 6.959   1.00 18.35 ? 300  PHE A CZ    1 
ATOM   2224 N N     . ASP A 1 301 ? -7.173  -26.053 4.674   1.00 17.24 ? 301  ASP A N     1 
ATOM   2225 C CA    . ASP A 1 301 ? -6.153  -25.981 5.713   1.00 15.97 ? 301  ASP A CA    1 
ATOM   2226 C C     . ASP A 1 301 ? -6.166  -24.614 6.399   1.00 13.92 ? 301  ASP A C     1 
ATOM   2227 O O     . ASP A 1 301 ? -5.994  -24.544 7.610   1.00 13.59 ? 301  ASP A O     1 
ATOM   2228 C CB    . ASP A 1 301 ? -4.781  -26.356 5.177   1.00 18.58 ? 301  ASP A CB    1 
ATOM   2229 C CG    . ASP A 1 301 ? -4.666  -27.797 4.692   1.00 19.63 ? 301  ASP A CG    1 
ATOM   2230 O OD1   . ASP A 1 301 ? -5.464  -28.650 5.139   1.00 21.46 ? 301  ASP A OD1   1 
ATOM   2231 O OD2   . ASP A 1 301 ? -3.743  -28.044 3.905   1.00 23.43 ? 301  ASP A OD2   1 
ATOM   2232 N N     . PHE A 1 302 ? -6.226  -23.532 5.628   1.00 14.00 ? 302  PHE A N     1 
ATOM   2233 C CA    . PHE A 1 302 ? -6.280  -22.185 6.199   1.00 13.42 ? 302  PHE A CA    1 
ATOM   2234 C C     . PHE A 1 302 ? -7.444  -22.090 7.199   1.00 14.48 ? 302  PHE A C     1 
ATOM   2235 O O     . PHE A 1 302 ? -7.319  -21.567 8.305   1.00 12.86 ? 302  PHE A O     1 
ATOM   2236 C CB    . PHE A 1 302 ? -6.498  -21.211 5.041   1.00 14.65 ? 302  PHE A CB    1 
ATOM   2237 C CG    . PHE A 1 302 ? -6.987  -19.846 5.474   1.00 16.69 ? 302  PHE A CG    1 
ATOM   2238 C CD1   . PHE A 1 302 ? -6.102  -18.886 5.939   1.00 19.00 ? 302  PHE A CD1   1 
ATOM   2239 C CD2   . PHE A 1 302 ? -8.331  -19.524 5.412   1.00 18.15 ? 302  PHE A CD2   1 
ATOM   2240 C CE1   . PHE A 1 302 ? -6.539  -17.633 6.307   1.00 18.90 ? 302  PHE A CE1   1 
ATOM   2241 C CE2   . PHE A 1 302 ? -8.783  -18.287 5.849   1.00 19.99 ? 302  PHE A CE2   1 
ATOM   2242 C CZ    . PHE A 1 302 ? -7.880  -17.336 6.288   1.00 21.06 ? 302  PHE A CZ    1 
ATOM   2243 N N     . SER A 1 303 ? -8.599  -22.609 6.768   1.00 15.65 ? 303  SER A N     1 
ATOM   2244 C CA    . SER A 1 303 ? -9.818  -22.504 7.560   1.00 14.11 ? 303  SER A CA    1 
ATOM   2245 C C     . SER A 1 303 ? -9.726  -23.366 8.823   1.00 14.23 ? 303  SER A C     1 
ATOM   2246 O O     . SER A 1 303 ? -10.145 -22.955 9.901   1.00 13.24 ? 303  SER A O     1 
ATOM   2247 C CB    . SER A 1 303 ? -11.043 -22.876 6.712   1.00 15.63 ? 303  SER A CB    1 
ATOM   2248 O OG    . SER A 1 303 ? -11.238 -22.065 5.550   1.00 16.63 ? 303  SER A OG    1 
ATOM   2249 N N     . ALA A 1 304 ? -9.243  -24.587 8.674   1.00 12.44 ? 304  ALA A N     1 
ATOM   2250 C CA    . ALA A 1 304 ? -9.043  -25.456 9.813   1.00 13.70 ? 304  ALA A CA    1 
ATOM   2251 C C     . ALA A 1 304 ? -8.092  -24.822 10.827  1.00 14.14 ? 304  ALA A C     1 
ATOM   2252 O O     . ALA A 1 304 ? -8.323  -24.905 12.051  1.00 14.98 ? 304  ALA A O     1 
ATOM   2253 C CB    . ALA A 1 304 ? -8.561  -26.815 9.368   1.00 13.60 ? 304  ALA A CB    1 
ATOM   2254 N N     . ALA A 1 305 ? -7.013  -24.191 10.323  1.00 15.44 ? 305  ALA A N     1 
ATOM   2255 C CA    . ALA A 1 305 ? -6.045  -23.585 11.221  1.00 16.77 ? 305  ALA A CA    1 
ATOM   2256 C C     . ALA A 1 305 ? -6.677  -22.406 11.954  1.00 15.46 ? 305  ALA A C     1 
ATOM   2257 O O     . ALA A 1 305 ? -6.445  -22.220 13.155  1.00 15.91 ? 305  ALA A O     1 
ATOM   2258 C CB    . ALA A 1 305 ? -4.790  -23.181 10.466  1.00 16.65 ? 305  ALA A CB    1 
ATOM   2259 N N     . ALA A 1 306 ? -7.512  -21.633 11.268  1.00 15.91 ? 306  ALA A N     1 
ATOM   2260 C CA    . ALA A 1 306 ? -8.176  -20.500 11.900  1.00 15.82 ? 306  ALA A CA    1 
ATOM   2261 C C     . ALA A 1 306 ? -9.110  -20.968 13.019  1.00 16.35 ? 306  ALA A C     1 
ATOM   2262 O O     . ALA A 1 306 ? -9.111  -20.372 14.102  1.00 16.63 ? 306  ALA A O     1 
ATOM   2263 C CB    . ALA A 1 306 ? -8.950  -19.685 10.892  1.00 16.52 ? 306  ALA A CB    1 
ATOM   2264 N N     . SER A 1 307 ? -9.865  -22.050 12.760  1.00 14.79 ? 307  SER A N     1 
ATOM   2265 C CA    . SER A 1 307 ? -10.732 -22.646 13.765  1.00 14.42 ? 307  SER A CA    1 
ATOM   2266 C C     . SER A 1 307 ? -9.925  -23.181 14.954  1.00 14.84 ? 307  SER A C     1 
ATOM   2267 O O     . SER A 1 307 ? -10.289 -22.924 16.093  1.00 15.38 ? 307  SER A O     1 
ATOM   2268 C CB    . SER A 1 307 ? -11.583 -23.757 13.190  1.00 14.95 ? 307  SER A CB    1 
ATOM   2269 O OG    . SER A 1 307 ? -12.540 -24.184 14.161  1.00 14.30 ? 307  SER A OG    1 
ATOM   2270 N N     . ALA A 1 308 ? -8.830  -23.912 14.680  1.00 15.01 ? 308  ALA A N     1 
ATOM   2271 C CA    . ALA A 1 308 ? -7.966  -24.439 15.727  1.00 17.74 ? 308  ALA A CA    1 
ATOM   2272 C C     . ALA A 1 308 ? -7.369  -23.328 16.600  1.00 17.52 ? 308  ALA A C     1 
ATOM   2273 O O     . ALA A 1 308 ? -7.294  -23.507 17.825  1.00 17.54 ? 308  ALA A O     1 
ATOM   2274 C CB    . ALA A 1 308 ? -6.915  -25.369 15.158  1.00 17.98 ? 308  ALA A CB    1 
ATOM   2275 N N     . GLN A 1 309 ? -7.014  -22.191 16.001  1.00 18.56 ? 309  GLN A N     1 
ATOM   2276 C CA    . GLN A 1 309 ? -6.432  -21.088 16.752  1.00 21.54 ? 309  GLN A CA    1 
ATOM   2277 C C     . GLN A 1 309 ? -7.419  -20.524 17.779  1.00 19.45 ? 309  GLN A C     1 
ATOM   2278 O O     . GLN A 1 309 ? -7.034  -20.252 18.922  1.00 20.32 ? 309  GLN A O     1 
ATOM   2279 C CB    . GLN A 1 309 ? -5.937  -20.033 15.774  1.00 24.54 ? 309  GLN A CB    1 
ATOM   2280 C CG    . GLN A 1 309 ? -5.363  -18.771 16.407  1.00 33.52 ? 309  GLN A CG    1 
ATOM   2281 C CD    . GLN A 1 309 ? -4.704  -17.887 15.364  1.00 42.73 ? 309  GLN A CD    1 
ATOM   2282 O OE1   . GLN A 1 309 ? -4.332  -18.342 14.275  1.00 43.60 ? 309  GLN A OE1   1 
ATOM   2283 N NE2   . GLN A 1 309 ? -4.544  -16.612 15.687  1.00 49.28 ? 309  GLN A NE2   1 
ATOM   2284 N N     . THR A 1 310 ? -8.679  -20.318 17.402  1.00 18.30 ? 310  THR A N     1 
ATOM   2285 C CA    . THR A 1 310 ? -9.635  -19.720 18.337  1.00 20.52 ? 310  THR A CA    1 
ATOM   2286 C C     . THR A 1 310 ? -9.972  -20.735 19.430  1.00 19.05 ? 310  THR A C     1 
ATOM   2287 O O     . THR A 1 310 ? -10.154 -20.366 20.589  1.00 20.13 ? 310  THR A O     1 
ATOM   2288 C CB    . THR A 1 310 ? -10.871 -19.205 17.590  1.00 26.28 ? 310  THR A CB    1 
ATOM   2289 O OG1   . THR A 1 310 ? -11.675 -20.326 17.234  1.00 27.13 ? 310  THR A OG1   1 
ATOM   2290 C CG2   . THR A 1 310 ? -10.494 -18.453 16.324  1.00 26.65 ? 310  THR A CG2   1 
ATOM   2291 N N     . LYS A 1 311 ? -9.974  -22.031 19.101  1.00 17.58 ? 311  LYS A N     1 
ATOM   2292 C CA    . LYS A 1 311 ? -10.216 -23.035 20.117  1.00 17.29 ? 311  LYS A CA    1 
ATOM   2293 C C     . LYS A 1 311 ? -9.062  -23.063 21.123  1.00 16.74 ? 311  LYS A C     1 
ATOM   2294 O O     . LYS A 1 311 ? -9.266  -23.097 22.343  1.00 16.77 ? 311  LYS A O     1 
ATOM   2295 C CB    . LYS A 1 311 ? -10.419 -24.414 19.499  1.00 20.42 ? 311  LYS A CB    1 
ATOM   2296 C CG    . LYS A 1 311 ? -10.771 -25.446 20.542  1.00 27.82 ? 311  LYS A CG    1 
ATOM   2297 C CD    . LYS A 1 311 ? -11.358 -26.747 20.016  1.00 34.60 ? 311  LYS A CD    1 
ATOM   2298 C CE    . LYS A 1 311 ? -10.310 -27.757 19.767  1.00 41.50 ? 311  LYS A CE    1 
ATOM   2299 N NZ    . LYS A 1 311 ? -10.935 -29.082 19.716  1.00 50.09 ? 311  LYS A NZ    1 
ATOM   2300 N N     . ALA A 1 312 ? -7.840  -23.021 20.595  1.00 18.28 ? 312  ALA A N     1 
ATOM   2301 C CA    . ALA A 1 312 ? -6.658  -22.980 21.447  1.00 19.14 ? 312  ALA A CA    1 
ATOM   2302 C C     . ALA A 1 312 ? -6.612  -21.730 22.325  1.00 17.94 ? 312  ALA A C     1 
ATOM   2303 O O     . ALA A 1 312 ? -6.004  -21.756 23.391  1.00 22.67 ? 312  ALA A O     1 
ATOM   2304 C CB    . ALA A 1 312 ? -5.412  -23.081 20.579  1.00 20.11 ? 312  ALA A CB    1 
ATOM   2305 N N     . ALA A 1 313 ? -7.153  -20.613 21.863  1.00 19.91 ? 313  ALA A N     1 
ATOM   2306 C CA    . ALA A 1 313 ? -7.169  -19.384 22.634  1.00 20.18 ? 313  ALA A CA    1 
ATOM   2307 C C     . ALA A 1 313 ? -8.039  -19.503 23.886  1.00 20.64 ? 313  ALA A C     1 
ATOM   2308 O O     . ALA A 1 313 ? -7.992  -18.632 24.741  1.00 22.18 ? 313  ALA A O     1 
ATOM   2309 C CB    . ALA A 1 313 ? -7.672  -18.229 21.796  1.00 20.70 ? 313  ALA A CB    1 
ATOM   2310 N N     . GLY A 1 314 ? -8.940  -20.478 23.937  1.00 17.00 ? 314  GLY A N     1 
ATOM   2311 C CA    . GLY A 1 314 ? -9.731  -20.649 25.139  1.00 18.01 ? 314  GLY A CA    1 
ATOM   2312 C C     . GLY A 1 314 ? -11.070 -19.917 25.141  1.00 17.61 ? 314  GLY A C     1 
ATOM   2313 O O     . GLY A 1 314 ? -11.744 -19.998 26.153  1.00 14.38 ? 314  GLY A O     1 
ATOM   2314 N N     . ILE A 1 315 ? -11.470 -19.293 24.018  1.00 17.40 ? 315  ILE A N     1 
ATOM   2315 C CA    . ILE A 1 315 ? -12.658 -18.451 23.971  1.00 18.60 ? 315  ILE A CA    1 
ATOM   2316 C C     . ILE A 1 315 ? -13.766 -19.075 23.115  1.00 17.45 ? 315  ILE A C     1 
ATOM   2317 O O     . ILE A 1 315 ? -14.737 -18.391 22.804  1.00 17.96 ? 315  ILE A O     1 
ATOM   2318 C CB    . ILE A 1 315 ? -12.289 -17.047 23.448  1.00 22.98 ? 315  ILE A CB    1 
ATOM   2319 C CG1   . ILE A 1 315 ? -11.810 -17.096 22.004  1.00 28.21 ? 315  ILE A CG1   1 
ATOM   2320 C CG2   . ILE A 1 315 ? -11.253 -16.396 24.374  1.00 25.35 ? 315  ILE A CG2   1 
ATOM   2321 C CD1   . ILE A 1 315 ? -11.668 -15.728 21.341  1.00 30.14 ? 315  ILE A CD1   1 
ATOM   2322 N N     . ALA A 1 316 ? -13.617 -20.332 22.715  1.00 14.82 ? 316  ALA A N     1 
ATOM   2323 C CA    . ALA A 1 316 ? -14.494 -20.878 21.688  1.00 16.03 ? 316  ALA A CA    1 
ATOM   2324 C C     . ALA A 1 316 ? -15.027 -22.241 22.084  1.00 16.32 ? 316  ALA A C     1 
ATOM   2325 O O     . ALA A 1 316 ? -15.424 -22.991 21.211  1.00 16.59 ? 316  ALA A O     1 
ATOM   2326 C CB    . ALA A 1 316 ? -13.773 -20.942 20.366  1.00 17.95 ? 316  ALA A CB    1 
ATOM   2327 N N     . SER A 1 317 ? -15.150 -22.503 23.391  1.00 15.84 ? 317  SER A N     1 
ATOM   2328 C CA    . SER A 1 317 ? -15.624 -23.790 23.878  1.00 16.56 ? 317  SER A CA    1 
ATOM   2329 C C     . SER A 1 317 ? -16.801 -23.578 24.830  1.00 15.16 ? 317  SER A C     1 
ATOM   2330 O O     . SER A 1 317 ? -16.856 -22.574 25.529  1.00 14.85 ? 317  SER A O     1 
ATOM   2331 C CB    . SER A 1 317 ? -14.530 -24.503 24.627  1.00 19.77 ? 317  SER A CB    1 
ATOM   2332 O OG    . SER A 1 317 ? -13.451 -24.806 23.749  1.00 21.84 ? 317  SER A OG    1 
ATOM   2333 N N     . PRO A 1 318 ? -17.700 -24.560 24.981  1.00 13.59 ? 318  PRO A N     1 
ATOM   2334 C CA    . PRO A 1 318 ? -18.730 -24.488 26.023  1.00 12.24 ? 318  PRO A CA    1 
ATOM   2335 C C     . PRO A 1 318 ? -17.996 -24.216 27.333  1.00 13.00 ? 318  PRO A C     1 
ATOM   2336 O O     . PRO A 1 318 ? -17.000 -24.885 27.593  1.00 14.27 ? 318  PRO A O     1 
ATOM   2337 C CB    . PRO A 1 318 ? -19.391 -25.879 25.952  1.00 13.58 ? 318  PRO A CB    1 
ATOM   2338 C CG    . PRO A 1 318 ? -19.250 -26.200 24.458  1.00 14.06 ? 318  PRO A CG    1 
ATOM   2339 C CD    . PRO A 1 318 ? -17.811 -25.779 24.147  1.00 14.35 ? 318  PRO A CD    1 
ATOM   2340 N N     . SER A 1 319 ? -18.490 -23.272 28.139  1.00 12.33 ? 319  SER A N     1 
ATOM   2341 C CA    . SER A 1 319 ? -17.776 -22.801 29.319  1.00 12.73 ? 319  SER A CA    1 
ATOM   2342 C C     . SER A 1 319 ? -18.658 -21.905 30.179  1.00 12.39 ? 319  SER A C     1 
ATOM   2343 O O     . SER A 1 319 ? -19.754 -21.547 29.793  1.00 12.09 ? 319  SER A O     1 
ATOM   2344 C CB    . SER A 1 319 ? -16.511 -22.103 28.916  1.00 14.33 ? 319  SER A CB    1 
ATOM   2345 O OG    . SER A 1 319 ? -16.778 -21.028 28.019  1.00 16.53 ? 319  SER A OG    1 
ATOM   2346 N N     . HIS A 1 320 ? -18.130 -21.519 31.347  1.00 12.88 ? 320  HIS A N     1 
ATOM   2347 C CA    . HIS A 1 320 ? -18.698 -20.480 32.172  1.00 12.64 ? 320  HIS A CA    1 
ATOM   2348 C C     . HIS A 1 320 ? -18.135 -19.149 31.674  1.00 12.41 ? 320  HIS A C     1 
ATOM   2349 O O     . HIS A 1 320 ? -16.913 -18.989 31.601  1.00 13.67 ? 320  HIS A O     1 
ATOM   2350 C CB    . HIS A 1 320 ? -18.352 -20.686 33.648  1.00 12.47 ? 320  HIS A CB    1 
ATOM   2351 C CG    . HIS A 1 320 ? -18.902 -21.916 34.292  1.00 12.01 ? 320  HIS A CG    1 
ATOM   2352 N ND1   . HIS A 1 320 ? -20.169 -21.950 34.826  1.00 13.04 ? 320  HIS A ND1   1 
ATOM   2353 C CD2   . HIS A 1 320 ? -18.426 -23.177 34.403  1.00 13.09 ? 320  HIS A CD2   1 
ATOM   2354 C CE1   . HIS A 1 320 ? -20.405 -23.167 35.320  1.00 13.05 ? 320  HIS A CE1   1 
ATOM   2355 N NE2   . HIS A 1 320 ? -19.396 -23.930 35.083  1.00 12.43 ? 320  HIS A NE2   1 
ATOM   2356 N N     . PHE A 1 321 ? -19.031 -18.224 31.319  1.00 12.09 ? 321  PHE A N     1 
ATOM   2357 C CA    . PHE A 1 321 ? -18.596 -16.947 30.821  1.00 11.98 ? 321  PHE A CA    1 
ATOM   2358 C C     . PHE A 1 321 ? -19.727 -15.930 30.776  1.00 11.37 ? 321  PHE A C     1 
ATOM   2359 O O     . PHE A 1 321 ? -20.923 -16.216 30.915  1.00 13.35 ? 321  PHE A O     1 
ATOM   2360 C CB    . PHE A 1 321 ? -18.011 -17.102 29.401  1.00 12.21 ? 321  PHE A CB    1 
ATOM   2361 C CG    . PHE A 1 321 ? -19.018 -17.477 28.325  1.00 11.58 ? 321  PHE A CG    1 
ATOM   2362 C CD1   . PHE A 1 321 ? -19.766 -16.508 27.672  1.00 11.97 ? 321  PHE A CD1   1 
ATOM   2363 C CD2   . PHE A 1 321 ? -19.215 -18.801 27.950  1.00 10.43 ? 321  PHE A CD2   1 
ATOM   2364 C CE1   . PHE A 1 321 ? -20.674 -16.847 26.687  1.00 11.67 ? 321  PHE A CE1   1 
ATOM   2365 C CE2   . PHE A 1 321 ? -20.136 -19.134 26.985  1.00 11.16 ? 321  PHE A CE2   1 
ATOM   2366 C CZ    . PHE A 1 321 ? -20.867 -18.156 26.350  1.00 11.32 ? 321  PHE A CZ    1 
ATOM   2367 N N     . TYR A 1 322 ? -19.319 -14.698 30.521  1.00 11.91 ? 322  TYR A N     1 
ATOM   2368 C CA    . TYR A 1 322 ? -20.236 -13.664 30.091  1.00 12.36 ? 322  TYR A CA    1 
ATOM   2369 C C     . TYR A 1 322 ? -19.589 -13.009 28.859  1.00 12.40 ? 322  TYR A C     1 
ATOM   2370 O O     . TYR A 1 322 ? -18.382 -13.106 28.686  1.00 12.59 ? 322  TYR A O     1 
ATOM   2371 C CB    . TYR A 1 322 ? -20.515 -12.651 31.203  1.00 12.95 ? 322  TYR A CB    1 
ATOM   2372 C CG    . TYR A 1 322 ? -21.512 -11.544 30.867  1.00 12.81 ? 322  TYR A CG    1 
ATOM   2373 C CD1   . TYR A 1 322 ? -22.669 -11.780 30.115  1.00 12.75 ? 322  TYR A CD1   1 
ATOM   2374 C CD2   . TYR A 1 322 ? -21.287 -10.246 31.281  1.00 12.57 ? 322  TYR A CD2   1 
ATOM   2375 C CE1   . TYR A 1 322 ? -23.522 -10.752 29.766  1.00 12.56 ? 322  TYR A CE1   1 
ATOM   2376 C CE2   . TYR A 1 322 ? -22.156 -9.213  30.963  1.00 12.01 ? 322  TYR A CE2   1 
ATOM   2377 C CZ    . TYR A 1 322 ? -23.281 -9.463  30.214  1.00 11.89 ? 322  TYR A CZ    1 
ATOM   2378 O OH    . TYR A 1 322 ? -24.103 -8.409  29.907  1.00 14.51 ? 322  TYR A OH    1 
ATOM   2379 N N     . ALA A 1 323 ? -20.380 -12.325 28.039  1.00 11.83 ? 323  ALA A N     1 
ATOM   2380 C CA    . ALA A 1 323 ? -19.900 -11.737 26.798  1.00 12.17 ? 323  ALA A CA    1 
ATOM   2381 C C     . ALA A 1 323 ? -20.871 -10.640 26.355  1.00 11.63 ? 323  ALA A C     1 
ATOM   2382 O O     . ALA A 1 323 ? -22.084 -10.787 26.539  1.00 11.81 ? 323  ALA A O     1 
ATOM   2383 C CB    . ALA A 1 323 ? -19.811 -12.822 25.732  1.00 12.12 ? 323  ALA A CB    1 
ATOM   2384 N N     . LYS A 1 324 ? -20.307 -9.572  25.756  1.00 11.37 ? 324  LYS A N     1 
ATOM   2385 C CA    . LYS A 1 324 ? -21.079 -8.434  25.271  1.00 11.72 ? 324  LYS A CA    1 
ATOM   2386 C C     . LYS A 1 324 ? -20.566 -8.026  23.894  1.00 11.32 ? 324  LYS A C     1 
ATOM   2387 O O     . LYS A 1 324 ? -19.498 -8.468  23.485  1.00 11.49 ? 324  LYS A O     1 
ATOM   2388 C CB    . LYS A 1 324 ? -20.990 -7.238  26.225  1.00 12.26 ? 324  LYS A CB    1 
ATOM   2389 C CG    . LYS A 1 324 ? -21.492 -7.512  27.655  1.00 11.62 ? 324  LYS A CG    1 
ATOM   2390 C CD    . LYS A 1 324 ? -21.464 -6.273  28.540  1.00 12.49 ? 324  LYS A CD    1 
ATOM   2391 C CE    . LYS A 1 324 ? -22.547 -5.228  28.263  1.00 13.19 ? 324  LYS A CE    1 
ATOM   2392 N NZ    . LYS A 1 324 ? -23.870 -5.628  28.772  1.00 13.97 ? 324  LYS A NZ    1 
ATOM   2393 N N     . SER A 1 325 ? -21.359 -7.235  23.159  1.00 11.68 ? 325  SER A N     1 
ATOM   2394 C CA    . SER A 1 325 ? -20.917 -6.744  21.851  1.00 12.34 ? 325  SER A CA    1 
ATOM   2395 C C     . SER A 1 325 ? -21.342 -5.301  21.678  1.00 12.88 ? 325  SER A C     1 
ATOM   2396 O O     . SER A 1 325 ? -22.303 -4.834  22.306  1.00 11.58 ? 325  SER A O     1 
ATOM   2397 C CB    . SER A 1 325 ? -21.430 -7.592  20.661  1.00 13.81 ? 325  SER A CB    1 
ATOM   2398 O OG    . SER A 1 325 ? -22.821 -7.358  20.379  1.00 15.49 ? 325  SER A OG    1 
ATOM   2399 N N     . LEU A 1 326 ? -20.628 -4.651  20.757  1.00 12.38 ? 326  LEU A N     1 
ATOM   2400 C CA    . LEU A 1 326 ? -20.925 -3.277  20.351  1.00 13.57 ? 326  LEU A CA    1 
ATOM   2401 C C     . LEU A 1 326 ? -20.570 -3.130  18.883  1.00 13.03 ? 326  LEU A C     1 
ATOM   2402 O O     . LEU A 1 326 ? -19.643 -3.781  18.425  1.00 13.32 ? 326  LEU A O     1 
ATOM   2403 C CB    . LEU A 1 326 ? -20.167 -2.210  21.139  1.00 13.69 ? 326  LEU A CB    1 
ATOM   2404 C CG    . LEU A 1 326 ? -20.562 -1.995  22.598  1.00 14.18 ? 326  LEU A CG    1 
ATOM   2405 C CD1   . LEU A 1 326 ? -19.482 -1.113  23.258  1.00 15.63 ? 326  LEU A CD1   1 
ATOM   2406 C CD2   . LEU A 1 326 ? -21.929 -1.396  22.687  1.00 15.65 ? 326  LEU A CD2   1 
ATOM   2407 N N     . VAL A 1 327 ? -21.257 -2.209  18.188  1.00 12.33 ? 327  VAL A N     1 
ATOM   2408 C CA    . VAL A 1 327 ? -20.907 -1.820  16.832  1.00 12.64 ? 327  VAL A CA    1 
ATOM   2409 C C     . VAL A 1 327 ? -20.405 -0.375  16.870  1.00 11.99 ? 327  VAL A C     1 
ATOM   2410 O O     . VAL A 1 327 ? -21.067 0.470   17.462  1.00 13.88 ? 327  VAL A O     1 
ATOM   2411 C CB    . VAL A 1 327 ? -22.140 -1.947  15.919  1.00 13.64 ? 327  VAL A CB    1 
ATOM   2412 C CG1   . VAL A 1 327 ? -21.833 -1.398  14.527  1.00 14.87 ? 327  VAL A CG1   1 
ATOM   2413 C CG2   . VAL A 1 327 ? -22.657 -3.381  15.852  1.00 14.08 ? 327  VAL A CG2   1 
ATOM   2414 N N     . PHE A 1 328 ? -19.304 -0.102  16.160  1.00 12.38 ? 328  PHE A N     1 
ATOM   2415 C CA    . PHE A 1 328 ? -18.757 1.235   16.018  1.00 12.71 ? 328  PHE A CA    1 
ATOM   2416 C C     . PHE A 1 328 ? -18.771 1.569   14.538  1.00 13.55 ? 328  PHE A C     1 
ATOM   2417 O O     . PHE A 1 328 ? -18.582 0.680   13.718  1.00 13.58 ? 328  PHE A O     1 
ATOM   2418 C CB    . PHE A 1 328 ? -17.345 1.336   16.602  1.00 12.99 ? 328  PHE A CB    1 
ATOM   2419 C CG    . PHE A 1 328 ? -17.358 1.237   18.121  1.00 12.64 ? 328  PHE A CG    1 
ATOM   2420 C CD1   . PHE A 1 328 ? -17.265 -0.004  18.759  1.00 13.03 ? 328  PHE A CD1   1 
ATOM   2421 C CD2   . PHE A 1 328 ? -17.462 2.371   18.914  1.00 13.72 ? 328  PHE A CD2   1 
ATOM   2422 C CE1   . PHE A 1 328 ? -17.335 -0.095  20.139  1.00 12.98 ? 328  PHE A CE1   1 
ATOM   2423 C CE2   . PHE A 1 328 ? -17.486 2.292   20.300  1.00 14.07 ? 328  PHE A CE2   1 
ATOM   2424 C CZ    . PHE A 1 328 ? -17.439 1.049   20.918  1.00 12.89 ? 328  PHE A CZ    1 
ATOM   2425 N N     . ASN A 1 329 ? -18.978 2.852   14.227  1.00 14.72 ? 329  ASN A N     1 
ATOM   2426 C CA    . ASN A 1 329 ? -18.941 3.329   12.847  1.00 14.36 ? 329  ASN A CA    1 
ATOM   2427 C C     . ASN A 1 329 ? -18.162 4.644   12.782  1.00 16.27 ? 329  ASN A C     1 
ATOM   2428 O O     . ASN A 1 329 ? -17.654 5.133   13.787  1.00 15.17 ? 329  ASN A O     1 
ATOM   2429 C CB    . ASN A 1 329 ? -20.354 3.396   12.291  1.00 15.00 ? 329  ASN A CB    1 
ATOM   2430 C CG    . ASN A 1 329 ? -21.237 4.332   13.078  1.00 15.52 ? 329  ASN A CG    1 
ATOM   2431 O OD1   . ASN A 1 329 ? -20.876 5.494   13.344  1.00 15.16 ? 329  ASN A OD1   1 
ATOM   2432 N ND2   . ASN A 1 329 ? -22.404 3.855   13.471  1.00 15.03 ? 329  ASN A ND2   1 
ATOM   2433 N N     . GLN A 1 330 ? -18.050 5.216   11.581  1.00 15.31 ? 330  GLN A N     1 
ATOM   2434 C CA    . GLN A 1 330 ? -17.215 6.389   11.389  1.00 17.42 ? 330  GLN A CA    1 
ATOM   2435 C C     . GLN A 1 330 ? -17.670 7.543   12.286  1.00 17.71 ? 330  GLN A C     1 
ATOM   2436 O O     . GLN A 1 330 ? -16.852 8.364   12.689  1.00 19.06 ? 330  GLN A O     1 
ATOM   2437 C CB    . GLN A 1 330 ? -17.315 6.844   9.935   1.00 19.74 ? 330  GLN A CB    1 
ATOM   2438 C CG    . GLN A 1 330 ? -16.424 8.042   9.593   1.00 23.16 ? 330  GLN A CG    1 
ATOM   2439 C CD    . GLN A 1 330 ? -14.951 7.778   9.801   1.00 23.31 ? 330  GLN A CD    1 
ATOM   2440 O OE1   . GLN A 1 330 ? -14.433 6.671   9.607   1.00 23.51 ? 330  GLN A OE1   1 
ATOM   2441 N NE2   . GLN A 1 330 ? -14.247 8.820   10.210  1.00 28.77 ? 330  GLN A NE2   1 
ATOM   2442 N N     . GLN A 1 331 ? -18.958 7.584   12.652  1.00 15.92 ? 331  GLN A N     1 
ATOM   2443 C CA    . GLN A 1 331 ? -19.500 8.644   13.492  1.00 17.76 ? 331  GLN A CA    1 
ATOM   2444 C C     . GLN A 1 331 ? -19.303 8.406   14.985  1.00 17.29 ? 331  GLN A C     1 
ATOM   2445 O O     . GLN A 1 331 ? -19.432 9.364   15.737  1.00 16.77 ? 331  GLN A O     1 
ATOM   2446 C CB    . GLN A 1 331 ? -20.985 8.887   13.266  1.00 20.17 ? 331  GLN A CB    1 
ATOM   2447 C CG    . GLN A 1 331 ? -21.239 9.642   11.964  1.00 21.26 ? 331  GLN A CG    1 
ATOM   2448 C CD    . GLN A 1 331 ? -20.939 8.818   10.729  1.00 22.85 ? 331  GLN A CD    1 
ATOM   2449 O OE1   . GLN A 1 331 ? -21.517 7.743   10.507  1.00 25.85 ? 331  GLN A OE1   1 
ATOM   2450 N NE2   . GLN A 1 331 ? -19.970 9.278   9.956   1.00 23.98 ? 331  GLN A NE2   1 
ATOM   2451 N N     . THR A 1 332 ? -18.959 7.166   15.391  1.00 16.32 ? 332  THR A N     1 
ATOM   2452 C CA    . THR A 1 332 ? -18.825 6.814   16.798  1.00 14.45 ? 332  THR A CA    1 
ATOM   2453 C C     . THR A 1 332 ? -17.448 6.220   17.132  1.00 13.68 ? 332  THR A C     1 
ATOM   2454 O O     . THR A 1 332 ? -17.285 5.563   18.157  1.00 14.63 ? 332  THR A O     1 
ATOM   2455 C CB    . THR A 1 332 ? -19.949 5.854   17.201  1.00 15.18 ? 332  THR A CB    1 
ATOM   2456 O OG1   . THR A 1 332 ? -19.845 4.668   16.418  1.00 14.35 ? 332  THR A OG1   1 
ATOM   2457 C CG2   . THR A 1 332 ? -21.328 6.444   16.974  1.00 15.50 ? 332  THR A CG2   1 
ATOM   2458 N N     . LEU A 1 333 ? -16.432 6.490   16.316  1.00 14.23 ? 333  LEU A N     1 
ATOM   2459 C CA    . LEU A 1 333 ? -15.075 6.060   16.568  1.00 15.69 ? 333  LEU A CA    1 
ATOM   2460 C C     . LEU A 1 333 ? -14.653 6.542   17.949  1.00 15.41 ? 333  LEU A C     1 
ATOM   2461 O O     . LEU A 1 333 ? -15.020 7.627   18.396  1.00 16.31 ? 333  LEU A O     1 
ATOM   2462 C CB    . LEU A 1 333 ? -14.094 6.576   15.515  1.00 16.90 ? 333  LEU A CB    1 
ATOM   2463 C CG    . LEU A 1 333 ? -14.347 6.091   14.084  1.00 17.50 ? 333  LEU A CG    1 
ATOM   2464 C CD1   . LEU A 1 333 ? -13.290 6.744   13.211  1.00 19.22 ? 333  LEU A CD1   1 
ATOM   2465 C CD2   . LEU A 1 333 ? -14.302 4.595   13.961  1.00 18.29 ? 333  LEU A CD2   1 
ATOM   2466 N N     . ILE A 1 334 ? -13.903 5.682   18.621  1.00 14.43 ? 334  ILE A N     1 
ATOM   2467 C CA    . ILE A 1 334 ? -13.556 5.908   20.012  1.00 13.84 ? 334  ILE A CA    1 
ATOM   2468 C C     . ILE A 1 334 ? -12.496 7.009   20.101  1.00 14.46 ? 334  ILE A C     1 
ATOM   2469 O O     . ILE A 1 334 ? -11.420 6.882   19.524  1.00 15.78 ? 334  ILE A O     1 
ATOM   2470 C CB    . ILE A 1 334 ? -13.091 4.603   20.665  1.00 12.77 ? 334  ILE A CB    1 
ATOM   2471 C CG1   . ILE A 1 334 ? -14.201 3.539   20.647  1.00 13.44 ? 334  ILE A CG1   1 
ATOM   2472 C CG2   . ILE A 1 334 ? -12.585 4.909   22.083  1.00 14.16 ? 334  ILE A CG2   1 
ATOM   2473 C CD1   . ILE A 1 334 ? -13.781 2.202   21.246  1.00 13.36 ? 334  ILE A CD1   1 
ATOM   2474 N N     . PRO A 1 335 ? -12.777 8.117   20.820  1.00 15.52 ? 335  PRO A N     1 
ATOM   2475 C CA    . PRO A 1 335 ? -11.801 9.201   20.962  1.00 14.91 ? 335  PRO A CA    1 
ATOM   2476 C C     . PRO A 1 335 ? -10.558 8.762   21.719  1.00 15.85 ? 335  PRO A C     1 
ATOM   2477 O O     . PRO A 1 335 ? -10.597 7.798   22.485  1.00 15.42 ? 335  PRO A O     1 
ATOM   2478 C CB    . PRO A 1 335 ? -12.543 10.293  21.733  1.00 16.09 ? 335  PRO A CB    1 
ATOM   2479 C CG    . PRO A 1 335 ? -13.989 9.952   21.521  1.00 16.70 ? 335  PRO A CG    1 
ATOM   2480 C CD    . PRO A 1 335 ? -14.068 8.424   21.473  1.00 14.71 ? 335  PRO A CD    1 
ATOM   2481 N N     . ASP A 1 336 ? -9.476  9.511   21.515  1.00 15.40 ? 336  ASP A N     1 
ATOM   2482 C CA    . ASP A 1 336 ? -8.208  9.245   22.180  1.00 15.87 ? 336  ASP A CA    1 
ATOM   2483 C C     . ASP A 1 336 ? -8.355  9.054   23.696  1.00 17.35 ? 336  ASP A C     1 
ATOM   2484 O O     . ASP A 1 336 ? -7.878  8.077   24.281  1.00 17.12 ? 336  ASP A O     1 
ATOM   2485 C CB    . ASP A 1 336 ? -7.246  10.385  21.900  1.00 16.97 ? 336  ASP A CB    1 
ATOM   2486 C CG    . ASP A 1 336 ? -6.747  10.497  20.472  1.00 19.54 ? 336  ASP A CG    1 
ATOM   2487 O OD1   . ASP A 1 336 ? -7.202  9.670   19.612  1.00 18.61 ? 336  ASP A OD1   1 
ATOM   2488 O OD2   . ASP A 1 336 ? -5.884  11.395  20.225  1.00 18.96 ? 336  ASP A OD2   1 
ATOM   2489 N N     . ASP A 1 337 ? -8.984  10.014  24.363  1.00 18.65 ? 337  ASP A N     1 
ATOM   2490 C CA    . ASP A 1 337 ? -9.083  9.945   25.809  1.00 20.29 ? 337  ASP A CA    1 
ATOM   2491 C C     . ASP A 1 337 ? -9.907  8.743   26.271  1.00 17.19 ? 337  ASP A C     1 
ATOM   2492 O O     . ASP A 1 337 ? -9.590  8.087   27.261  1.00 15.60 ? 337  ASP A O     1 
ATOM   2493 C CB    . ASP A 1 337 ? -9.671  11.219  26.373  1.00 22.58 ? 337  ASP A CB    1 
ATOM   2494 C CG    . ASP A 1 337 ? -9.530  11.296  27.886  1.00 28.84 ? 337  ASP A CG    1 
ATOM   2495 O OD1   . ASP A 1 337 ? -8.369  11.351  28.359  1.00 34.45 ? 337  ASP A OD1   1 
ATOM   2496 O OD2   . ASP A 1 337 ? -10.562 11.228  28.568  1.00 30.94 ? 337  ASP A OD2   1 
ATOM   2497 N N     . ALA A 1 338 ? -11.020 8.464   25.593  1.00 16.35 ? 338  ALA A N     1 
ATOM   2498 C CA    . ALA A 1 338 ? -11.815 7.313   25.977  1.00 15.51 ? 338  ALA A CA    1 
ATOM   2499 C C     . ALA A 1 338 ? -11.001 6.029   25.810  1.00 14.25 ? 338  ALA A C     1 
ATOM   2500 O O     . ALA A 1 338 ? -11.071 5.119   26.648  1.00 15.25 ? 338  ALA A O     1 
ATOM   2501 C CB    . ALA A 1 338 ? -13.117 7.301   25.197  1.00 15.80 ? 338  ALA A CB    1 
ATOM   2502 N N     . ALA A 1 339 ? -10.230 5.916   24.724  1.00 14.20 ? 339  ALA A N     1 
ATOM   2503 C CA    . ALA A 1 339 ? -9.394  4.732   24.531  1.00 14.69 ? 339  ALA A CA    1 
ATOM   2504 C C     . ALA A 1 339 ? -8.400  4.590   25.684  1.00 15.28 ? 339  ALA A C     1 
ATOM   2505 O O     . ALA A 1 339 ? -8.199  3.507   26.217  1.00 14.62 ? 339  ALA A O     1 
ATOM   2506 C CB    . ALA A 1 339 ? -8.643  4.786   23.232  1.00 14.56 ? 339  ALA A CB    1 
ATOM   2507 N N     . GLU A 1 340 ? -7.833  5.703   26.133  1.00 14.78 ? 340  GLU A N     1 
ATOM   2508 C CA    . GLU A 1 340 ? -6.921  5.628   27.268  1.00 15.85 ? 340  GLU A CA    1 
ATOM   2509 C C     . GLU A 1 340 ? -7.660  5.078   28.496  1.00 14.87 ? 340  GLU A C     1 
ATOM   2510 O O     . GLU A 1 340 ? -7.130  4.234   29.197  1.00 16.36 ? 340  GLU A O     1 
ATOM   2511 C CB    . GLU A 1 340 ? -6.355  7.010   27.587  1.00 17.41 ? 340  GLU A CB    1 
ATOM   2512 C CG    . GLU A 1 340 ? -5.434  7.533   26.496  1.00 21.35 ? 340  GLU A CG    1 
ATOM   2513 C CD    . GLU A 1 340 ? -4.105  6.816   26.230  1.00 28.93 ? 340  GLU A CD    1 
ATOM   2514 O OE1   . GLU A 1 340 ? -3.654  5.906   27.000  1.00 28.30 ? 340  GLU A OE1   1 
ATOM   2515 O OE2   . GLU A 1 340 ? -3.485  7.185   25.191  1.00 33.60 ? 340  GLU A OE2   1 
ATOM   2516 N N     . GLU A 1 341 ? -8.884  5.541   28.723  1.00 14.97 ? 341  GLU A N     1 
ATOM   2517 C CA    . GLU A 1 341 ? -9.710  5.109   29.847  1.00 15.46 ? 341  GLU A CA    1 
ATOM   2518 C C     . GLU A 1 341 ? -10.097 3.632   29.697  1.00 15.21 ? 341  GLU A C     1 
ATOM   2519 O O     . GLU A 1 341 ? -10.132 2.907   30.686  1.00 15.13 ? 341  GLU A O     1 
ATOM   2520 C CB    . GLU A 1 341 ? -10.923 6.008   30.037  1.00 17.51 ? 341  GLU A CB    1 
ATOM   2521 C CG    . GLU A 1 341 ? -10.591 7.435   30.466  1.00 20.25 ? 341  GLU A CG    1 
ATOM   2522 C CD    . GLU A 1 341 ? -9.840  7.499   31.797  1.00 23.51 ? 341  GLU A CD    1 
ATOM   2523 O OE1   . GLU A 1 341 ? -9.009  8.420   31.921  1.00 31.10 ? 341  GLU A OE1   1 
ATOM   2524 O OE2   . GLU A 1 341 ? -10.021 6.615   32.688  1.00 25.71 ? 341  GLU A OE2   1 
ATOM   2525 N N     . VAL A 1 342 ? -10.357 3.170   28.466  1.00 14.35 ? 342  VAL A N     1 
ATOM   2526 C CA    . VAL A 1 342 ? -10.663 1.763   28.230  1.00 14.46 ? 342  VAL A CA    1 
ATOM   2527 C C     . VAL A 1 342 ? -9.548  0.880   28.772  1.00 15.02 ? 342  VAL A C     1 
ATOM   2528 O O     . VAL A 1 342 ? -9.818  -0.087  29.482  1.00 14.39 ? 342  VAL A O     1 
ATOM   2529 C CB    . VAL A 1 342 ? -10.918 1.460   26.749  1.00 14.37 ? 342  VAL A CB    1 
ATOM   2530 C CG1   . VAL A 1 342 ? -10.882 -0.034  26.463  1.00 13.20 ? 342  VAL A CG1   1 
ATOM   2531 C CG2   . VAL A 1 342 ? -12.231 2.096   26.314  1.00 14.81 ? 342  VAL A CG2   1 
ATOM   2532 N N     . PHE A 1 343 ? -8.306  1.185   28.386  1.00 14.72 ? 343  PHE A N     1 
ATOM   2533 C CA    . PHE A 1 343 ? -7.198  0.323   28.738  1.00 14.15 ? 343  PHE A CA    1 
ATOM   2534 C C     . PHE A 1 343 ? -6.821  0.480   30.210  1.00 15.70 ? 343  PHE A C     1 
ATOM   2535 O O     . PHE A 1 343 ? -6.343  -0.499  30.803  1.00 15.51 ? 343  PHE A O     1 
ATOM   2536 C CB    . PHE A 1 343 ? -6.067  0.560   27.730  1.00 13.50 ? 343  PHE A CB    1 
ATOM   2537 C CG    . PHE A 1 343 ? -6.476  -0.146  26.446  1.00 14.16 ? 343  PHE A CG    1 
ATOM   2538 C CD1   . PHE A 1 343 ? -6.325  -1.520  26.314  1.00 14.87 ? 343  PHE A CD1   1 
ATOM   2539 C CD2   . PHE A 1 343 ? -7.048  0.560   25.407  1.00 14.68 ? 343  PHE A CD2   1 
ATOM   2540 C CE1   . PHE A 1 343 ? -6.751  -2.175  25.182  1.00 15.68 ? 343  PHE A CE1   1 
ATOM   2541 C CE2   . PHE A 1 343 ? -7.494  -0.102  24.288  1.00 14.20 ? 343  PHE A CE2   1 
ATOM   2542 C CZ    . PHE A 1 343 ? -7.335  -1.463  24.172  1.00 14.93 ? 343  PHE A CZ    1 
ATOM   2543 N N     . LYS A 1 344 ? -7.007  1.668   30.786  1.00 15.20 ? 344  LYS A N     1 
ATOM   2544 C CA    . LYS A 1 344 ? -6.881  1.835   32.237  1.00 16.62 ? 344  LYS A CA    1 
ATOM   2545 C C     . LYS A 1 344 ? -7.887  0.953   32.974  1.00 16.57 ? 344  LYS A C     1 
ATOM   2546 O O     . LYS A 1 344 ? -7.542  0.268   33.949  1.00 16.77 ? 344  LYS A O     1 
ATOM   2547 C CB    . LYS A 1 344 ? -6.982  3.312   32.628  1.00 18.12 ? 344  LYS A CB    1 
ATOM   2548 C CG    . LYS A 1 344 ? -5.704  4.068   32.330  1.00 23.66 ? 344  LYS A CG    1 
ATOM   2549 C CD    . LYS A 1 344 ? -5.648  5.435   33.009  1.00 30.35 ? 344  LYS A CD    1 
ATOM   2550 C CE    . LYS A 1 344 ? -6.547  6.466   32.446  1.00 37.81 ? 344  LYS A CE    1 
ATOM   2551 N NZ    . LYS A 1 344 ? -6.860  7.489   33.464  1.00 43.72 ? 344  LYS A NZ    1 
ATOM   2552 N N     . TYR A 1 345 ? -9.121  0.926   32.464  1.00 15.18 ? 345  TYR A N     1 
ATOM   2553 C CA    . TYR A 1 345 ? -10.183 0.149   33.067  1.00 14.10 ? 345  TYR A CA    1 
ATOM   2554 C C     . TYR A 1 345 ? -9.816  -1.342  33.039  1.00 14.19 ? 345  TYR A C     1 
ATOM   2555 O O     . TYR A 1 345 ? -9.959  -2.031  34.051  1.00 14.25 ? 345  TYR A O     1 
ATOM   2556 C CB    . TYR A 1 345 ? -11.503 0.424   32.321  1.00 14.00 ? 345  TYR A CB    1 
ATOM   2557 C CG    . TYR A 1 345 ? -12.688 -0.400  32.797  1.00 13.30 ? 345  TYR A CG    1 
ATOM   2558 C CD1   . TYR A 1 345 ? -12.913 -1.698  32.329  1.00 12.97 ? 345  TYR A CD1   1 
ATOM   2559 C CD2   . TYR A 1 345 ? -13.559 0.107   33.737  1.00 13.15 ? 345  TYR A CD2   1 
ATOM   2560 C CE1   . TYR A 1 345 ? -13.957 -2.465  32.804  1.00 12.39 ? 345  TYR A CE1   1 
ATOM   2561 C CE2   . TYR A 1 345 ? -14.631 -0.635  34.204  1.00 14.64 ? 345  TYR A CE2   1 
ATOM   2562 C CZ    . TYR A 1 345 ? -14.829 -1.932  33.734  1.00 13.43 ? 345  TYR A CZ    1 
ATOM   2563 O OH    . TYR A 1 345 ? -15.871 -2.660  34.217  1.00 14.55 ? 345  TYR A OH    1 
ATOM   2564 N N     . LEU A 1 346 ? -9.331  -1.828  31.890  1.00 14.30 ? 346  LEU A N     1 
ATOM   2565 C CA    . LEU A 1 346 ? -8.936  -3.222  31.759  1.00 14.03 ? 346  LEU A CA    1 
ATOM   2566 C C     . LEU A 1 346 ? -7.776  -3.550  32.701  1.00 15.51 ? 346  LEU A C     1 
ATOM   2567 O O     . LEU A 1 346 ? -7.672  -4.680  33.239  1.00 15.16 ? 346  LEU A O     1 
ATOM   2568 C CB    . LEU A 1 346 ? -8.542  -3.525  30.313  1.00 14.24 ? 346  LEU A CB    1 
ATOM   2569 C CG    . LEU A 1 346 ? -9.701  -3.554  29.315  1.00 15.20 ? 346  LEU A CG    1 
ATOM   2570 C CD1   . LEU A 1 346 ? -9.179  -3.749  27.915  1.00 15.97 ? 346  LEU A CD1   1 
ATOM   2571 C CD2   . LEU A 1 346 ? -10.694 -4.650  29.676  1.00 15.50 ? 346  LEU A CD2   1 
ATOM   2572 N N     . ALA A 1 347 ? -6.902  -2.555  32.890  1.00 16.58 ? 347  ALA A N     1 
ATOM   2573 C CA    . ALA A 1 347 ? -5.697  -2.757  33.687  1.00 17.76 ? 347  ALA A CA    1 
ATOM   2574 C C     . ALA A 1 347 ? -6.045  -2.963  35.166  1.00 19.86 ? 347  ALA A C     1 
ATOM   2575 O O     . ALA A 1 347 ? -5.380  -3.769  35.817  1.00 23.03 ? 347  ALA A O     1 
ATOM   2576 C CB    . ALA A 1 347 ? -4.742  -1.584  33.547  1.00 16.97 ? 347  ALA A CB    1 
ATOM   2577 N N     . THR A 1 348 ? -7.012  -2.208  35.714  1.00 18.05 ? 348  THR A N     1 
ATOM   2578 C CA    . THR A 1 348 ? -7.170  -2.139  37.166  1.00 18.91 ? 348  THR A CA    1 
ATOM   2579 C C     . THR A 1 348 ? -8.470  -2.768  37.678  1.00 17.82 ? 348  THR A C     1 
ATOM   2580 O O     . THR A 1 348 ? -8.539  -3.141  38.854  1.00 18.90 ? 348  THR A O     1 
ATOM   2581 C CB    . THR A 1 348 ? -6.999  -0.703  37.655  1.00 20.92 ? 348  THR A CB    1 
ATOM   2582 O OG1   . THR A 1 348 ? -8.036  0.080   37.092  1.00 21.87 ? 348  THR A OG1   1 
ATOM   2583 C CG2   . THR A 1 348 ? -5.668  -0.099  37.258  1.00 25.75 ? 348  THR A CG2   1 
ATOM   2584 N N     . THR A 1 349 ? -9.515  -2.920  36.850  1.00 15.92 ? 349  THR A N     1 
ATOM   2585 C CA    . THR A 1 349 ? -10.800 -3.376  37.372  1.00 14.57 ? 349  THR A CA    1 
ATOM   2586 C C     . THR A 1 349 ? -10.704 -4.848  37.823  1.00 15.31 ? 349  THR A C     1 
ATOM   2587 O O     . THR A 1 349 ? -10.179 -5.697  37.102  1.00 16.05 ? 349  THR A O     1 
ATOM   2588 C CB    . THR A 1 349 ? -11.904 -3.204  36.317  1.00 14.54 ? 349  THR A CB    1 
ATOM   2589 O OG1   . THR A 1 349 ? -11.877 -1.833  35.929  1.00 15.95 ? 349  THR A OG1   1 
ATOM   2590 C CG2   . THR A 1 349 ? -13.270 -3.522  36.888  1.00 14.36 ? 349  THR A CG2   1 
ATOM   2591 N N     . LYS A 1 350 ? -11.269 -5.155  38.989  1.00 15.95 ? 350  LYS A N     1 
ATOM   2592 C CA    . LYS A 1 350 ? -11.393 -6.552  39.425  1.00 20.25 ? 350  LYS A CA    1 
ATOM   2593 C C     . LYS A 1 350 ? -12.339 -7.287  38.466  1.00 17.03 ? 350  LYS A C     1 
ATOM   2594 O O     . LYS A 1 350 ? -13.477 -6.869  38.258  1.00 19.42 ? 350  LYS A O     1 
ATOM   2595 C CB    . LYS A 1 350 ? -11.886 -6.576  40.886  1.00 25.07 ? 350  LYS A CB    1 
ATOM   2596 C CG    . LYS A 1 350 ? -10.861 -6.065  41.925  1.00 33.69 ? 350  LYS A CG    1 
ATOM   2597 C CD    . LYS A 1 350 ? -9.517  -6.803  42.035  1.00 41.54 ? 350  LYS A CD    1 
ATOM   2598 C CE    . LYS A 1 350 ? -8.377  -6.134  42.832  1.00 43.28 ? 350  LYS A CE    1 
ATOM   2599 N NZ    . LYS A 1 350 ? -7.065  -6.214  42.138  1.00 36.70 ? 350  LYS A NZ    1 
ATOM   2600 N N     . ASN A 1 351 ? -11.840 -8.325  37.791  1.00 15.17 ? 351  ASN A N     1 
ATOM   2601 C CA    . ASN A 1 351 ? -12.584 -8.878  36.670  1.00 15.33 ? 351  ASN A CA    1 
ATOM   2602 C C     . ASN A 1 351 ? -13.180 -10.261 36.947  1.00 15.70 ? 351  ASN A C     1 
ATOM   2603 O O     . ASN A 1 351 ? -14.102 -10.675 36.247  1.00 15.58 ? 351  ASN A O     1 
ATOM   2604 C CB    . ASN A 1 351 ? -11.765 -8.768  35.383  1.00 14.71 ? 351  ASN A CB    1 
ATOM   2605 C CG    . ASN A 1 351 ? -10.512 -9.593  35.383  1.00 15.83 ? 351  ASN A CG    1 
ATOM   2606 O OD1   . ASN A 1 351 ? -10.575 -10.785 35.706  1.00 14.85 ? 351  ASN A OD1   1 
ATOM   2607 N ND2   . ASN A 1 351 ? -9.382  -9.014  34.967  1.00 15.71 ? 351  ASN A ND2   1 
ATOM   2608 N N     . GLY A 1 352 ? -12.621 -11.031 37.866  1.00 15.16 ? 352  GLY A N     1 
ATOM   2609 C CA    . GLY A 1 352 ? -13.179 -12.323 38.217  1.00 15.16 ? 352  GLY A CA    1 
ATOM   2610 C C     . GLY A 1 352 ? -12.915 -13.426 37.198  1.00 14.38 ? 352  GLY A C     1 
ATOM   2611 O O     . GLY A 1 352 ? -13.454 -14.525 37.363  1.00 14.44 ? 352  GLY A O     1 
ATOM   2612 N N     . THR A 1 353 ? -12.144 -13.121 36.151  1.00 14.60 ? 353  THR A N     1 
ATOM   2613 C CA    . THR A 1 353 ? -11.977 -14.032 35.030  1.00 14.58 ? 353  THR A CA    1 
ATOM   2614 C C     . THR A 1 353 ? -10.754 -14.907 35.228  1.00 15.99 ? 353  THR A C     1 
ATOM   2615 O O     . THR A 1 353 ? -9.809  -14.514 35.916  1.00 16.80 ? 353  THR A O     1 
ATOM   2616 C CB    . THR A 1 353 ? -11.902 -13.297 33.687  1.00 14.78 ? 353  THR A CB    1 
ATOM   2617 O OG1   . THR A 1 353 ? -10.661 -12.584 33.574  1.00 14.48 ? 353  THR A OG1   1 
ATOM   2618 C CG2   . THR A 1 353 ? -13.101 -12.378 33.491  1.00 13.77 ? 353  THR A CG2   1 
ATOM   2619 N N     . ASP A 1 354 ? -10.746 -16.054 34.529  1.00 16.45 ? 354  ASP A N     1 
ATOM   2620 C CA    . ASP A 1 354 ? -9.526  -16.812 34.311  1.00 16.67 ? 354  ASP A CA    1 
ATOM   2621 C C     . ASP A 1 354 ? -8.937  -16.529 32.926  1.00 17.00 ? 354  ASP A C     1 
ATOM   2622 O O     . ASP A 1 354 ? -7.776  -16.842 32.664  1.00 16.50 ? 354  ASP A O     1 
ATOM   2623 C CB    . ASP A 1 354 ? -9.720  -18.300 34.607  1.00 17.88 ? 354  ASP A CB    1 
ATOM   2624 C CG    . ASP A 1 354 ? -10.494 -19.126 33.592  1.00 20.31 ? 354  ASP A CG    1 
ATOM   2625 O OD1   . ASP A 1 354 ? -11.147 -18.545 32.724  1.00 17.05 ? 354  ASP A OD1   1 
ATOM   2626 O OD2   . ASP A 1 354 ? -10.448 -20.377 33.669  1.00 22.31 ? 354  ASP A OD2   1 
ATOM   2627 N N     . LEU A 1 355 ? -9.734  -15.908 32.048  1.00 14.56 ? 355  LEU A N     1 
ATOM   2628 C CA    . LEU A 1 355 ? -9.301  -15.435 30.744  1.00 15.07 ? 355  LEU A CA    1 
ATOM   2629 C C     . LEU A 1 355 ? -10.276 -14.358 30.292  1.00 15.05 ? 355  LEU A C     1 
ATOM   2630 O O     . LEU A 1 355 ? -11.482 -14.507 30.473  1.00 14.40 ? 355  LEU A O     1 
ATOM   2631 C CB    . LEU A 1 355 ? -9.365  -16.651 29.821  1.00 19.18 ? 355  LEU A CB    1 
ATOM   2632 C CG    . LEU A 1 355 ? -9.178  -16.435 28.328  1.00 27.14 ? 355  LEU A CG    1 
ATOM   2633 C CD1   . LEU A 1 355 ? -7.898  -15.684 28.083  1.00 30.41 ? 355  LEU A CD1   1 
ATOM   2634 C CD2   . LEU A 1 355 ? -9.184  -17.809 27.682  1.00 27.90 ? 355  LEU A CD2   1 
ATOM   2635 N N     . TYR A 1 356 ? -9.785  -13.293 29.658  1.00 14.23 ? 356  TYR A N     1 
ATOM   2636 C CA    . TYR A 1 356 ? -10.686 -12.425 28.915  1.00 13.38 ? 356  TYR A CA    1 
ATOM   2637 C C     . TYR A 1 356 ? -10.053 -12.102 27.559  1.00 13.63 ? 356  TYR A C     1 
ATOM   2638 O O     . TYR A 1 356 ? -8.836  -12.147 27.381  1.00 13.70 ? 356  TYR A O     1 
ATOM   2639 C CB    . TYR A 1 356 ? -11.093 -11.133 29.661  1.00 14.28 ? 356  TYR A CB    1 
ATOM   2640 C CG    . TYR A 1 356 ? -10.044 -10.034 29.768  1.00 15.13 ? 356  TYR A CG    1 
ATOM   2641 C CD1   . TYR A 1 356 ? -9.830  -9.169  28.706  1.00 15.57 ? 356  TYR A CD1   1 
ATOM   2642 C CD2   . TYR A 1 356 ? -9.288  -9.828  30.928  1.00 15.71 ? 356  TYR A CD2   1 
ATOM   2643 C CE1   . TYR A 1 356 ? -8.880  -8.160  28.753  1.00 17.26 ? 356  TYR A CE1   1 
ATOM   2644 C CE2   . TYR A 1 356 ? -8.347  -8.816  30.992  1.00 16.05 ? 356  TYR A CE2   1 
ATOM   2645 C CZ    . TYR A 1 356 ? -8.125  -7.982  29.902  1.00 16.79 ? 356  TYR A CZ    1 
ATOM   2646 O OH    . TYR A 1 356 ? -7.174  -6.988  29.961  1.00 17.10 ? 356  TYR A OH    1 
ATOM   2647 N N     . ALA A 1 357 ? -10.915 -11.698 26.614  1.00 13.18 ? 357  ALA A N     1 
ATOM   2648 C CA    . ALA A 1 357 ? -10.511 -11.198 25.313  1.00 13.45 ? 357  ALA A CA    1 
ATOM   2649 C C     . ALA A 1 357 ? -11.483 -10.100 24.907  1.00 15.94 ? 357  ALA A C     1 
ATOM   2650 O O     . ALA A 1 357 ? -12.697 -10.247 25.100  1.00 16.09 ? 357  ALA A O     1 
ATOM   2651 C CB    . ALA A 1 357 ? -10.512 -12.304 24.308  1.00 13.43 ? 357  ALA A CB    1 
ATOM   2652 N N     . VAL A 1 358 ? -10.914 -8.998  24.404  1.00 14.51 ? 358  VAL A N     1 
ATOM   2653 C CA    . VAL A 1 358 ? -11.655 -7.900  23.808  1.00 14.62 ? 358  VAL A CA    1 
ATOM   2654 C C     . VAL A 1 358 ? -11.231 -7.850  22.340  1.00 15.04 ? 358  VAL A C     1 
ATOM   2655 O O     . VAL A 1 358 ? -10.091 -7.585  22.030  1.00 12.66 ? 358  VAL A O     1 
ATOM   2656 C CB    . VAL A 1 358 ? -11.419 -6.571  24.554  1.00 15.12 ? 358  VAL A CB    1 
ATOM   2657 C CG1   . VAL A 1 358 ? -12.258 -5.438  23.983  1.00 15.93 ? 358  VAL A CG1   1 
ATOM   2658 C CG2   . VAL A 1 358 ? -11.714 -6.702  26.044  1.00 15.87 ? 358  VAL A CG2   1 
ATOM   2659 N N     . THR A 1 359 ? -12.145 -8.231  21.445  1.00 13.98 ? 359  THR A N     1 
ATOM   2660 C CA    . THR A 1 359 ? -11.831 -8.381  20.034  1.00 14.20 ? 359  THR A CA    1 
ATOM   2661 C C     . THR A 1 359 ? -12.475 -7.234  19.271  1.00 14.15 ? 359  THR A C     1 
ATOM   2662 O O     . THR A 1 359 ? -13.707 -7.055  19.352  1.00 14.46 ? 359  THR A O     1 
ATOM   2663 C CB    . THR A 1 359 ? -12.363 -9.724  19.541  1.00 14.90 ? 359  THR A CB    1 
ATOM   2664 O OG1   . THR A 1 359 ? -11.729 -10.790 20.245  1.00 15.95 ? 359  THR A OG1   1 
ATOM   2665 C CG2   . THR A 1 359 ? -12.154 -9.935  18.055  1.00 16.66 ? 359  THR A CG2   1 
ATOM   2666 N N     . PHE A 1 360 ? -11.655 -6.539  18.486  1.00 12.59 ? 360  PHE A N     1 
ATOM   2667 C CA    . PHE A 1 360 ? -12.127 -5.556  17.530  1.00 13.74 ? 360  PHE A CA    1 
ATOM   2668 C C     . PHE A 1 360 ? -11.993 -6.193  16.152  1.00 13.01 ? 360  PHE A C     1 
ATOM   2669 O O     . PHE A 1 360 ? -10.882 -6.524  15.741  1.00 14.01 ? 360  PHE A O     1 
ATOM   2670 C CB    . PHE A 1 360 ? -11.324 -4.278  17.728  1.00 13.96 ? 360  PHE A CB    1 
ATOM   2671 C CG    . PHE A 1 360 ? -11.345 -3.682  19.132  1.00 12.80 ? 360  PHE A CG    1 
ATOM   2672 C CD1   . PHE A 1 360 ? -12.334 -2.786  19.523  1.00 13.73 ? 360  PHE A CD1   1 
ATOM   2673 C CD2   . PHE A 1 360 ? -10.358 -4.005  20.044  1.00 13.44 ? 360  PHE A CD2   1 
ATOM   2674 C CE1   . PHE A 1 360 ? -12.329 -2.245  20.785  1.00 13.30 ? 360  PHE A CE1   1 
ATOM   2675 C CE2   . PHE A 1 360 ? -10.353 -3.449  21.304  1.00 13.72 ? 360  PHE A CE2   1 
ATOM   2676 C CZ    . PHE A 1 360 ? -11.346 -2.571  21.666  1.00 13.34 ? 360  PHE A CZ    1 
ATOM   2677 N N     . ALA A 1 361 ? -13.110 -6.327  15.421  1.00 12.57 ? 361  ALA A N     1 
ATOM   2678 C CA    . ALA A 1 361 ? -13.094 -7.030  14.145  1.00 13.11 ? 361  ALA A CA    1 
ATOM   2679 C C     . ALA A 1 361 ? -13.630 -6.097  13.074  1.00 12.52 ? 361  ALA A C     1 
ATOM   2680 O O     . ALA A 1 361 ? -14.793 -5.698  13.137  1.00 12.96 ? 361  ALA A O     1 
ATOM   2681 C CB    . ALA A 1 361 ? -13.922 -8.268  14.216  1.00 13.48 ? 361  ALA A CB    1 
ATOM   2682 N N     . ALA A 1 362 ? -12.748 -5.767  12.142  1.00 13.20 ? 362  ALA A N     1 
ATOM   2683 C CA    . ALA A 1 362 ? -13.123 -4.836  11.074  1.00 13.18 ? 362  ALA A CA    1 
ATOM   2684 C C     . ALA A 1 362 ? -14.190 -5.423  10.161  1.00 13.65 ? 362  ALA A C     1 
ATOM   2685 O O     . ALA A 1 362 ? -14.115 -6.595  9.753   1.00 13.17 ? 362  ALA A O     1 
ATOM   2686 C CB    . ALA A 1 362 ? -11.921 -4.462  10.255  1.00 12.54 ? 362  ALA A CB    1 
ATOM   2687 N N     . LEU A 1 363 ? -15.152 -4.566  9.857   1.00 14.68 ? 363  LEU A N     1 
ATOM   2688 C CA    . LEU A 1 363 ? -16.134 -4.935  8.830   1.00 13.55 ? 363  LEU A CA    1 
ATOM   2689 C C     . LEU A 1 363 ? -15.841 -3.899  7.739   1.00 13.36 ? 363  LEU A C     1 
ATOM   2690 O O     . LEU A 1 363 ? -14.718 -3.447  7.637   1.00 14.60 ? 363  LEU A O     1 
ATOM   2691 C CB    . LEU A 1 363 ? -17.557 -4.772  9.350   1.00 15.38 ? 363  LEU A CB    1 
ATOM   2692 C CG    . LEU A 1 363 ? -17.930 -5.749  10.468  1.00 17.63 ? 363  LEU A CG    1 
ATOM   2693 C CD1   . LEU A 1 363 ? -19.144 -5.298  11.250  1.00 20.24 ? 363  LEU A CD1   1 
ATOM   2694 C CD2   . LEU A 1 363 ? -18.129 -7.139  9.891   1.00 19.96 ? 363  LEU A CD2   1 
ATOM   2695 N N     . GLY A 1 364 ? -16.854 -3.584  6.963   1.00 13.28 ? 364  GLY A N     1 
ATOM   2696 C CA    . GLY A 1 364 ? -16.637 -2.664  5.849   1.00 14.28 ? 364  GLY A CA    1 
ATOM   2697 C C     . GLY A 1 364 ? -16.369 -3.547  4.651   1.00 14.29 ? 364  GLY A C     1 
ATOM   2698 O O     . GLY A 1 364 ? -16.783 -4.711  4.639   1.00 14.28 ? 364  GLY A O     1 
ATOM   2699 N N     . GLY A 1 365 ? -15.660 -2.997  3.685   1.00 15.83 ? 365  GLY A N     1 
ATOM   2700 C CA    . GLY A 1 365 ? -15.484 -3.754  2.450   1.00 16.10 ? 365  GLY A CA    1 
ATOM   2701 C C     . GLY A 1 365 ? -16.821 -4.128  1.834   1.00 14.96 ? 365  GLY A C     1 
ATOM   2702 O O     . GLY A 1 365 ? -17.719 -3.289  1.810   1.00 15.17 ? 365  GLY A O     1 
ATOM   2703 N N     . ALA A 1 366 ? -16.935 -5.376  1.401   1.00 13.84 ? 366  ALA A N     1 
ATOM   2704 C CA    . ALA A 1 366 ? -18.106 -5.872  0.703   1.00 15.35 ? 366  ALA A CA    1 
ATOM   2705 C C     . ALA A 1 366 ? -19.321 -5.981  1.621   1.00 14.34 ? 366  ALA A C     1 
ATOM   2706 O O     . ALA A 1 366 ? -20.454 -6.090  1.149   1.00 15.45 ? 366  ALA A O     1 
ATOM   2707 C CB    . ALA A 1 366 ? -17.810 -7.227  0.072   1.00 15.30 ? 366  ALA A CB    1 
ATOM   2708 N N     . VAL A 1 367 ? -19.107 -5.972  2.943   1.00 15.01 ? 367  VAL A N     1 
ATOM   2709 C CA    . VAL A 1 367 ? -20.247 -5.977  3.843   1.00 14.91 ? 367  VAL A CA    1 
ATOM   2710 C C     . VAL A 1 367 ? -21.151 -4.777  3.550   1.00 15.06 ? 367  VAL A C     1 
ATOM   2711 O O     . VAL A 1 367 ? -22.381 -4.862  3.623   1.00 15.00 ? 367  VAL A O     1 
ATOM   2712 C CB    . VAL A 1 367 ? -19.834 -5.989  5.322   1.00 14.54 ? 367  VAL A CB    1 
ATOM   2713 C CG1   . VAL A 1 367 ? -21.060 -5.914  6.226   1.00 13.60 ? 367  VAL A CG1   1 
ATOM   2714 C CG2   . VAL A 1 367 ? -19.019 -7.232  5.628   1.00 15.60 ? 367  VAL A CG2   1 
ATOM   2715 N N     . ARG A 1 368 ? -20.550 -3.648  3.172   1.00 15.68 ? 368  ARG A N     1 
ATOM   2716 C CA    . ARG A 1 368 ? -21.318 -2.426  3.024   1.00 18.88 ? 368  ARG A CA    1 
ATOM   2717 C C     . ARG A 1 368 ? -21.972 -2.384  1.636   1.00 19.53 ? 368  ARG A C     1 
ATOM   2718 O O     . ARG A 1 368 ? -22.671 -1.431  1.344   1.00 22.88 ? 368  ARG A O     1 
ATOM   2719 C CB    . ARG A 1 368 ? -20.441 -1.198  3.310   1.00 21.44 ? 368  ARG A CB    1 
ATOM   2720 C CG    . ARG A 1 368 ? -21.253 0.038   3.682   1.00 23.43 ? 368  ARG A CG    1 
ATOM   2721 C CD    . ARG A 1 368 ? -20.396 1.091   4.332   1.00 23.35 ? 368  ARG A CD    1 
ATOM   2722 N NE    . ARG A 1 368 ? -21.077 2.367   4.557   1.00 24.37 ? 368  ARG A NE    1 
ATOM   2723 C CZ    . ARG A 1 368 ? -20.462 3.389   5.140   1.00 23.61 ? 368  ARG A CZ    1 
ATOM   2724 N NH1   . ARG A 1 368 ? -21.113 4.520   5.386   1.00 27.35 ? 368  ARG A NH1   1 
ATOM   2725 N NH2   . ARG A 1 368 ? -19.193 3.287   5.479   1.00 25.38 ? 368  ARG A NH2   1 
ATOM   2726 N N     . ASP A 1 369 ? -21.806 -3.417  0.802   1.00 17.63 ? 369  ASP A N     1 
ATOM   2727 C CA    . ASP A 1 369 ? -22.339 -3.365  -0.559  1.00 18.33 ? 369  ASP A CA    1 
ATOM   2728 C C     . ASP A 1 369 ? -23.848 -3.574  -0.543  1.00 20.78 ? 369  ASP A C     1 
ATOM   2729 O O     . ASP A 1 369 ? -24.523 -3.364  -1.550  1.00 21.46 ? 369  ASP A O     1 
ATOM   2730 C CB    . ASP A 1 369 ? -21.736 -4.443  -1.446  1.00 19.92 ? 369  ASP A CB    1 
ATOM   2731 C CG    . ASP A 1 369 ? -20.276 -4.240  -1.830  1.00 21.90 ? 369  ASP A CG    1 
ATOM   2732 O OD1   . ASP A 1 369 ? -19.794 -3.095  -1.668  1.00 24.76 ? 369  ASP A OD1   1 
ATOM   2733 O OD2   . ASP A 1 369 ? -19.667 -5.226  -2.283  1.00 24.98 ? 369  ASP A OD2   1 
ATOM   2734 N N     . VAL A 1 370 ? -24.375 -4.049  0.588   1.00 18.28 ? 370  VAL A N     1 
ATOM   2735 C CA    . VAL A 1 370 ? -25.801 -4.227  0.802   1.00 18.60 ? 370  VAL A CA    1 
ATOM   2736 C C     . VAL A 1 370 ? -26.263 -3.205  1.821   1.00 20.76 ? 370  VAL A C     1 
ATOM   2737 O O     . VAL A 1 370 ? -25.579 -2.967  2.806   1.00 20.97 ? 370  VAL A O     1 
ATOM   2738 C CB    . VAL A 1 370 ? -26.035 -5.655  1.307   1.00 18.69 ? 370  VAL A CB    1 
ATOM   2739 C CG1   . VAL A 1 370 ? -27.490 -5.900  1.655   1.00 19.03 ? 370  VAL A CG1   1 
ATOM   2740 C CG2   . VAL A 1 370 ? -25.555 -6.668  0.282   1.00 20.22 ? 370  VAL A CG2   1 
ATOM   2741 N N     . SER A 1 371 ? -27.433 -2.622  1.575   1.00 19.55 ? 371  SER A N     1 
ATOM   2742 C CA    . SER A 1 371 ? -27.955 -1.563  2.415   1.00 18.75 ? 371  SER A CA    1 
ATOM   2743 C C     . SER A 1 371 ? -28.533 -2.135  3.708   1.00 15.86 ? 371  SER A C     1 
ATOM   2744 O O     . SER A 1 371 ? -28.978 -3.282  3.761   1.00 15.49 ? 371  SER A O     1 
ATOM   2745 C CB    . SER A 1 371 ? -28.978 -0.787  1.614   1.00 23.02 ? 371  SER A CB    1 
ATOM   2746 O OG    . SER A 1 371 ? -30.236 -0.674  2.225   1.00 25.87 ? 371  SER A OG    1 
ATOM   2747 N N     . ALA A 1 372 ? -28.541 -1.303  4.747   1.00 16.30 ? 372  ALA A N     1 
ATOM   2748 C CA    . ALA A 1 372 ? -29.139 -1.671  6.024   1.00 16.43 ? 372  ALA A CA    1 
ATOM   2749 C C     . ALA A 1 372 ? -30.571 -2.182  5.900   1.00 17.49 ? 372  ALA A C     1 
ATOM   2750 O O     . ALA A 1 372 ? -30.968 -3.019  6.691   1.00 17.59 ? 372  ALA A O     1 
ATOM   2751 C CB    . ALA A 1 372 ? -29.059 -0.500  6.965   1.00 15.79 ? 372  ALA A CB    1 
ATOM   2752 N N     . SER A 1 373 ? -31.350 -1.699  4.935   1.00 16.88 ? 373  SER A N     1 
ATOM   2753 C CA    . SER A 1 373 ? -32.752 -2.064  4.867   1.00 19.76 ? 373  SER A CA    1 
ATOM   2754 C C     . SER A 1 373 ? -33.011 -3.295  3.984   1.00 19.61 ? 373  SER A C     1 
ATOM   2755 O O     . SER A 1 373 ? -34.156 -3.746  3.896   1.00 21.89 ? 373  SER A O     1 
ATOM   2756 C CB    . SER A 1 373 ? -33.581 -0.868  4.435   1.00 23.64 ? 373  SER A CB    1 
ATOM   2757 O OG    . SER A 1 373 ? -33.263 -0.558  3.097   1.00 27.69 ? 373  SER A OG    1 
ATOM   2758 N N     . GLU A 1 374 ? -31.983 -3.863  3.337   1.00 18.41 ? 374  GLU A N     1 
ATOM   2759 C CA    . GLU A 1 374 ? -32.190 -4.946  2.377   1.00 19.49 ? 374  GLU A CA    1 
ATOM   2760 C C     . GLU A 1 374 ? -32.317 -6.304  3.067   1.00 18.03 ? 374  GLU A C     1 
ATOM   2761 O O     . GLU A 1 374 ? -32.886 -7.219  2.499   1.00 18.69 ? 374  GLU A O     1 
ATOM   2762 C CB    . GLU A 1 374 ? -31.083 -5.082  1.315   1.00 25.16 ? 374  GLU A CB    1 
ATOM   2763 C CG    . GLU A 1 374 ? -31.227 -6.307  0.386   1.00 34.27 ? 374  GLU A CG    1 
ATOM   2764 C CD    . GLU A 1 374 ? -30.128 -6.714  -0.619  1.00 47.03 ? 374  GLU A CD    1 
ATOM   2765 O OE1   . GLU A 1 374 ? -29.704 -5.784  -1.368  1.00 49.37 ? 374  GLU A OE1   1 
ATOM   2766 O OE2   . GLU A 1 374 ? -29.707 -7.933  -0.715  1.00 39.91 ? 374  GLU A OE2   1 
ATOM   2767 N N     . THR A 1 375 ? -31.681 -6.478  4.227   1.00 14.75 ? 375  THR A N     1 
ATOM   2768 C CA    . THR A 1 375 ? -31.766 -7.695  5.023   1.00 15.65 ? 375  THR A CA    1 
ATOM   2769 C C     . THR A 1 375 ? -31.967 -7.268  6.472   1.00 13.34 ? 375  THR A C     1 
ATOM   2770 O O     . THR A 1 375 ? -31.773 -6.107  6.802   1.00 13.42 ? 375  THR A O     1 
ATOM   2771 C CB    . THR A 1 375 ? -30.504 -8.578  4.919   1.00 15.06 ? 375  THR A CB    1 
ATOM   2772 O OG1   . THR A 1 375 ? -29.470 -8.033  5.737   1.00 14.56 ? 375  THR A OG1   1 
ATOM   2773 C CG2   . THR A 1 375 ? -30.015 -8.807  3.511   1.00 15.25 ? 375  THR A CG2   1 
ATOM   2774 N N     . ALA A 1 376 ? -32.342 -8.189  7.357   1.00 12.85 ? 376  ALA A N     1 
ATOM   2775 C CA    . ALA A 1 376 ? -32.576 -7.828  8.739   1.00 12.74 ? 376  ALA A CA    1 
ATOM   2776 C C     . ALA A 1 376 ? -31.292 -7.375  9.438   1.00 13.94 ? 376  ALA A C     1 
ATOM   2777 O O     . ALA A 1 376 ? -31.386 -6.691  10.439  1.00 15.17 ? 376  ALA A O     1 
ATOM   2778 C CB    . ALA A 1 376 ? -33.229 -8.997  9.496   1.00 13.36 ? 376  ALA A CB    1 
ATOM   2779 N N     . PHE A 1 377 ? -30.111 -7.746  8.925   1.00 14.50 ? 377  PHE A N     1 
ATOM   2780 C CA    . PHE A 1 377 ? -28.848 -7.276  9.473   1.00 13.38 ? 377  PHE A CA    1 
ATOM   2781 C C     . PHE A 1 377 ? -28.751 -5.772  9.254   1.00 13.15 ? 377  PHE A C     1 
ATOM   2782 O O     . PHE A 1 377 ? -28.637 -5.313  8.118   1.00 13.86 ? 377  PHE A O     1 
ATOM   2783 C CB    . PHE A 1 377 ? -27.676 -7.993  8.803   1.00 13.91 ? 377  PHE A CB    1 
ATOM   2784 C CG    . PHE A 1 377 ? -26.328 -7.604  9.378   1.00 14.80 ? 377  PHE A CG    1 
ATOM   2785 C CD1   . PHE A 1 377 ? -25.811 -8.301  10.460  1.00 15.34 ? 377  PHE A CD1   1 
ATOM   2786 C CD2   . PHE A 1 377 ? -25.579 -6.555  8.864   1.00 14.22 ? 377  PHE A CD2   1 
ATOM   2787 C CE1   . PHE A 1 377 ? -24.589 -7.946  11.012  1.00 15.34 ? 377  PHE A CE1   1 
ATOM   2788 C CE2   . PHE A 1 377 ? -24.375 -6.195  9.419   1.00 15.08 ? 377  PHE A CE2   1 
ATOM   2789 C CZ    . PHE A 1 377 ? -23.887 -6.872  10.513  1.00 14.64 ? 377  PHE A CZ    1 
ATOM   2790 N N     . TYR A 1 378 ? -28.759 -5.008  10.341  1.00 12.94 ? 378  TYR A N     1 
ATOM   2791 C CA    . TYR A 1 378 ? -28.870 -3.556  10.265  1.00 13.13 ? 378  TYR A CA    1 
ATOM   2792 C C     . TYR A 1 378 ? -27.520 -2.854  10.106  1.00 14.81 ? 378  TYR A C     1 
ATOM   2793 O O     . TYR A 1 378 ? -27.461 -1.772  9.500   1.00 14.34 ? 378  TYR A O     1 
ATOM   2794 C CB    . TYR A 1 378 ? -29.559 -3.038  11.530  1.00 13.81 ? 378  TYR A CB    1 
ATOM   2795 C CG    . TYR A 1 378 ? -29.782 -1.535  11.542  1.00 14.63 ? 378  TYR A CG    1 
ATOM   2796 C CD1   . TYR A 1 378 ? -30.648 -0.940  10.635  1.00 16.45 ? 378  TYR A CD1   1 
ATOM   2797 C CD2   . TYR A 1 378 ? -29.101 -0.719  12.420  1.00 15.14 ? 378  TYR A CD2   1 
ATOM   2798 C CE1   . TYR A 1 378 ? -30.803 0.439   10.584  1.00 17.63 ? 378  TYR A CE1   1 
ATOM   2799 C CE2   . TYR A 1 378 ? -29.267 0.650   12.401  1.00 18.11 ? 378  TYR A CE2   1 
ATOM   2800 C CZ    . TYR A 1 378 ? -30.121 1.234   11.476  1.00 18.46 ? 378  TYR A CZ    1 
ATOM   2801 O OH    . TYR A 1 378 ? -30.293 2.600   11.497  1.00 23.97 ? 378  TYR A OH    1 
ATOM   2802 N N     . HIS A 1 379 ? -26.435 -3.470  10.593  1.00 13.90 ? 379  HIS A N     1 
ATOM   2803 C CA    . HIS A 1 379 ? -25.197 -2.770  10.893  1.00 13.07 ? 379  HIS A CA    1 
ATOM   2804 C C     . HIS A 1 379 ? -24.259 -2.643  9.692   1.00 14.27 ? 379  HIS A C     1 
ATOM   2805 O O     . HIS A 1 379 ? -23.065 -2.844  9.804   1.00 13.54 ? 379  HIS A O     1 
ATOM   2806 C CB    . HIS A 1 379 ? -24.554 -3.450  12.097  1.00 13.18 ? 379  HIS A CB    1 
ATOM   2807 C CG    . HIS A 1 379 ? -25.539 -3.592  13.215  1.00 12.78 ? 379  HIS A CG    1 
ATOM   2808 N ND1   . HIS A 1 379 ? -26.092 -2.496  13.839  1.00 12.93 ? 379  HIS A ND1   1 
ATOM   2809 C CD2   . HIS A 1 379 ? -26.083 -4.678  13.785  1.00 12.67 ? 379  HIS A CD2   1 
ATOM   2810 C CE1   . HIS A 1 379 ? -26.971 -2.925  14.723  1.00 13.60 ? 379  HIS A CE1   1 
ATOM   2811 N NE2   . HIS A 1 379 ? -26.948 -4.264  14.753  1.00 13.98 ? 379  HIS A NE2   1 
ATOM   2812 N N     . ARG A 1 380 ? -24.807 -2.325  8.508   1.00 14.07 ? 380  ARG A N     1 
ATOM   2813 C CA    . ARG A 1 380 ? -24.015 -2.406  7.283   1.00 13.08 ? 380  ARG A CA    1 
ATOM   2814 C C     . ARG A 1 380 ? -22.959 -1.304  7.196   1.00 15.11 ? 380  ARG A C     1 
ATOM   2815 O O     . ARG A 1 380 ? -21.975 -1.469  6.475   1.00 14.50 ? 380  ARG A O     1 
ATOM   2816 C CB    . ARG A 1 380 ? -24.988 -2.285  6.109   1.00 13.15 ? 380  ARG A CB    1 
ATOM   2817 C CG    . ARG A 1 380 ? -25.867 -3.503  5.931   1.00 13.55 ? 380  ARG A CG    1 
ATOM   2818 C CD    . ARG A 1 380 ? -25.073 -4.674  5.468   1.00 15.17 ? 380  ARG A CD    1 
ATOM   2819 N NE    . ARG A 1 380 ? -25.935 -5.816  5.200   1.00 14.57 ? 380  ARG A NE    1 
ATOM   2820 C CZ    . ARG A 1 380 ? -25.547 -6.964  4.661   1.00 14.41 ? 380  ARG A CZ    1 
ATOM   2821 N NH1   . ARG A 1 380 ? -24.306 -7.171  4.218   1.00 15.26 ? 380  ARG A NH1   1 
ATOM   2822 N NH2   . ARG A 1 380 ? -26.448 -7.905  4.482   1.00 15.61 ? 380  ARG A NH2   1 
ATOM   2823 N N     . ASP A 1 381 ? -23.169 -0.154  7.846   1.00 13.95 ? 381  ASP A N     1 
ATOM   2824 C CA    . ASP A 1 381 ? -22.169 0.895   7.806   1.00 15.86 ? 381  ASP A CA    1 
ATOM   2825 C C     . ASP A 1 381 ? -21.155 0.768   8.941   1.00 14.78 ? 381  ASP A C     1 
ATOM   2826 O O     . ASP A 1 381 ? -20.412 1.707   9.226   1.00 14.44 ? 381  ASP A O     1 
ATOM   2827 C CB    . ASP A 1 381 ? -22.806 2.270   7.823   1.00 17.26 ? 381  ASP A CB    1 
ATOM   2828 C CG    . ASP A 1 381 ? -23.548 2.663   9.079   1.00 18.45 ? 381  ASP A CG    1 
ATOM   2829 O OD1   . ASP A 1 381 ? -23.776 1.802   9.942   1.00 16.97 ? 381  ASP A OD1   1 
ATOM   2830 O OD2   . ASP A 1 381 ? -23.912 3.850   9.164   1.00 21.23 ? 381  ASP A OD2   1 
ATOM   2831 N N     . ALA A 1 382 ? -21.127 -0.385  9.608   1.00 13.19 ? 382  ALA A N     1 
ATOM   2832 C CA    . ALA A 1 382 ? -20.210 -0.552  10.723  1.00 13.01 ? 382  ALA A CA    1 
ATOM   2833 C C     . ALA A 1 382 ? -18.785 -0.376  10.238  1.00 13.37 ? 382  ALA A C     1 
ATOM   2834 O O     . ALA A 1 382 ? -18.416 -0.854  9.162   1.00 14.89 ? 382  ALA A O     1 
ATOM   2835 C CB    . ALA A 1 382 ? -20.358 -1.914  11.363  1.00 12.64 ? 382  ALA A CB    1 
ATOM   2836 N N     . SER A 1 383 ? -17.958 0.215   11.105  1.00 12.11 ? 383  SER A N     1 
ATOM   2837 C CA    . SER A 1 383 ? -16.509 0.135   10.951  1.00 12.88 ? 383  SER A CA    1 
ATOM   2838 C C     . SER A 1 383 ? -15.959 -1.189  11.482  1.00 12.56 ? 383  SER A C     1 
ATOM   2839 O O     . SER A 1 383 ? -15.170 -1.875  10.839  1.00 13.50 ? 383  SER A O     1 
ATOM   2840 C CB    . SER A 1 383 ? -15.827 1.290   11.633  1.00 13.10 ? 383  SER A CB    1 
ATOM   2841 O OG    . SER A 1 383 ? -16.211 2.514   11.020  1.00 16.15 ? 383  SER A OG    1 
ATOM   2842 N N     . TYR A 1 384 ? -16.416 -1.555  12.673  1.00 12.46 ? 384  TYR A N     1 
ATOM   2843 C CA    . TYR A 1 384 ? -15.944 -2.770  13.319  1.00 11.74 ? 384  TYR A CA    1 
ATOM   2844 C C     . TYR A 1 384 ? -16.932 -3.194  14.407  1.00 11.60 ? 384  TYR A C     1 
ATOM   2845 O O     . TYR A 1 384 ? -17.683 -2.393  14.948  1.00 12.76 ? 384  TYR A O     1 
ATOM   2846 C CB    . TYR A 1 384 ? -14.534 -2.634  13.901  1.00 12.19 ? 384  TYR A CB    1 
ATOM   2847 C CG    . TYR A 1 384 ? -14.322 -1.484  14.881  1.00 12.47 ? 384  TYR A CG    1 
ATOM   2848 C CD1   . TYR A 1 384 ? -14.540 -1.642  16.247  1.00 12.47 ? 384  TYR A CD1   1 
ATOM   2849 C CD2   . TYR A 1 384 ? -13.920 -0.219  14.450  1.00 12.24 ? 384  TYR A CD2   1 
ATOM   2850 C CE1   . TYR A 1 384 ? -14.303 -0.611  17.157  1.00 13.50 ? 384  TYR A CE1   1 
ATOM   2851 C CE2   . TYR A 1 384 ? -13.707 0.829   15.345  1.00 13.53 ? 384  TYR A CE2   1 
ATOM   2852 C CZ    . TYR A 1 384 ? -13.889 0.629   16.712  1.00 13.83 ? 384  TYR A CZ    1 
ATOM   2853 O OH    . TYR A 1 384 ? -13.679 1.628   17.617  1.00 14.20 ? 384  TYR A OH    1 
ATOM   2854 N N     . PHE A 1 385 ? -16.901 -4.489  14.710  1.00 11.44 ? 385  PHE A N     1 
ATOM   2855 C CA    . PHE A 1 385 ? -17.490 -5.028  15.916  1.00 12.10 ? 385  PHE A CA    1 
ATOM   2856 C C     . PHE A 1 385 ? -16.471 -4.990  17.056  1.00 13.04 ? 385  PHE A C     1 
ATOM   2857 O O     . PHE A 1 385 ? -15.261 -5.145  16.846  1.00 13.05 ? 385  PHE A O     1 
ATOM   2858 C CB    . PHE A 1 385 ? -17.819 -6.501  15.694  1.00 13.32 ? 385  PHE A CB    1 
ATOM   2859 C CG    . PHE A 1 385 ? -19.009 -6.877  14.827  1.00 15.44 ? 385  PHE A CG    1 
ATOM   2860 C CD1   . PHE A 1 385 ? -20.246 -6.267  14.985  1.00 16.59 ? 385  PHE A CD1   1 
ATOM   2861 C CD2   . PHE A 1 385 ? -18.883 -7.935  13.915  1.00 16.26 ? 385  PHE A CD2   1 
ATOM   2862 C CE1   . PHE A 1 385 ? -21.336 -6.711  14.229  1.00 17.83 ? 385  PHE A CE1   1 
ATOM   2863 C CE2   . PHE A 1 385 ? -19.967 -8.350  13.158  1.00 15.89 ? 385  PHE A CE2   1 
ATOM   2864 C CZ    . PHE A 1 385 ? -21.171 -7.743  13.318  1.00 16.20 ? 385  PHE A CZ    1 
ATOM   2865 N N     . MET A 1 386 ? -16.995 -4.858  18.284  1.00 12.56 ? 386  MET A N     1 
ATOM   2866 C CA    . MET A 1 386 ? -16.274 -5.092  19.529  1.00 12.17 ? 386  MET A CA    1 
ATOM   2867 C C     . MET A 1 386 ? -16.991 -6.255  20.209  1.00 12.49 ? 386  MET A C     1 
ATOM   2868 O O     . MET A 1 386 ? -18.212 -6.193  20.408  1.00 12.54 ? 386  MET A O     1 
ATOM   2869 C CB    . MET A 1 386 ? -16.360 -3.886  20.467  1.00 12.48 ? 386  MET A CB    1 
ATOM   2870 C CG    . MET A 1 386 ? -15.506 -3.953  21.722  1.00 13.37 ? 386  MET A CG    1 
ATOM   2871 S SD    . MET A 1 386 ? -15.985 -5.197  22.939  1.00 14.17 ? 386  MET A SD    1 
ATOM   2872 C CE    . MET A 1 386 ? -17.664 -4.747  23.360  1.00 15.13 ? 386  MET A CE    1 
ATOM   2873 N N     . PHE A 1 387 ? -16.267 -7.350  20.402  1.00 12.37 ? 387  PHE A N     1 
ATOM   2874 C CA    . PHE A 1 387 ? -16.764 -8.450  21.207  1.00 12.11 ? 387  PHE A CA    1 
ATOM   2875 C C     . PHE A 1 387 ? -15.915 -8.579  22.460  1.00 12.14 ? 387  PHE A C     1 
ATOM   2876 O O     . PHE A 1 387 ? -14.703 -8.774  22.355  1.00 12.74 ? 387  PHE A O     1 
ATOM   2877 C CB    . PHE A 1 387 ? -16.702 -9.790  20.485  1.00 13.22 ? 387  PHE A CB    1 
ATOM   2878 C CG    . PHE A 1 387 ? -17.458 -9.755  19.153  1.00 14.58 ? 387  PHE A CG    1 
ATOM   2879 C CD1   . PHE A 1 387 ? -18.828 -9.563  19.122  1.00 15.36 ? 387  PHE A CD1   1 
ATOM   2880 C CD2   . PHE A 1 387 ? -16.801 -9.977  17.956  1.00 18.20 ? 387  PHE A CD2   1 
ATOM   2881 C CE1   . PHE A 1 387 ? -19.516 -9.554  17.911  1.00 16.22 ? 387  PHE A CE1   1 
ATOM   2882 C CE2   . PHE A 1 387 ? -17.502 -10.003 16.759  1.00 19.34 ? 387  PHE A CE2   1 
ATOM   2883 C CZ    . PHE A 1 387 ? -18.851 -9.802  16.746  1.00 17.13 ? 387  PHE A CZ    1 
ATOM   2884 N N     . SER A 1 388 ? -16.576 -8.604  23.617  1.00 11.39 ? 388  SER A N     1 
ATOM   2885 C CA    . SER A 1 388 ? -15.885 -8.835  24.882  1.00 11.66 ? 388  SER A CA    1 
ATOM   2886 C C     . SER A 1 388 ? -16.320 -10.191 25.409  1.00 11.60 ? 388  SER A C     1 
ATOM   2887 O O     . SER A 1 388 ? -17.495 -10.558 25.288  1.00 12.51 ? 388  SER A O     1 
ATOM   2888 C CB    . SER A 1 388 ? -16.129 -7.735  25.885  1.00 11.39 ? 388  SER A CB    1 
ATOM   2889 O OG    . SER A 1 388 ? -17.493 -7.599  26.260  1.00 11.83 ? 388  SER A OG    1 
ATOM   2890 N N     . PHE A 1 389 ? -15.369 -10.908 26.018  1.00 11.35 ? 389  PHE A N     1 
ATOM   2891 C CA    . PHE A 1 389 ? -15.583 -12.271 26.480  1.00 11.54 ? 389  PHE A CA    1 
ATOM   2892 C C     . PHE A 1 389 ? -14.813 -12.447 27.780  1.00 12.82 ? 389  PHE A C     1 
ATOM   2893 O O     . PHE A 1 389 ? -13.615 -12.198 27.829  1.00 14.05 ? 389  PHE A O     1 
ATOM   2894 C CB    . PHE A 1 389 ? -15.042 -13.253 25.457  1.00 12.82 ? 389  PHE A CB    1 
ATOM   2895 C CG    . PHE A 1 389 ? -15.352 -14.694 25.813  1.00 14.47 ? 389  PHE A CG    1 
ATOM   2896 C CD1   . PHE A 1 389 ? -16.545 -15.269 25.364  1.00 17.21 ? 389  PHE A CD1   1 
ATOM   2897 C CD2   . PHE A 1 389 ? -14.425 -15.490 26.473  1.00 19.19 ? 389  PHE A CD2   1 
ATOM   2898 C CE1   . PHE A 1 389 ? -16.828 -16.609 25.624  1.00 17.68 ? 389  PHE A CE1   1 
ATOM   2899 C CE2   . PHE A 1 389 ? -14.743 -16.831 26.754  1.00 18.71 ? 389  PHE A CE2   1 
ATOM   2900 C CZ    . PHE A 1 389 ? -15.957 -17.347 26.353  1.00 19.24 ? 389  PHE A CZ    1 
ATOM   2901 N N     . GLY A 1 390 ? -15.525 -12.833 28.839  1.00 11.85 ? 390  GLY A N     1 
ATOM   2902 C CA    . GLY A 1 390 ? -14.902 -13.007 30.141  1.00 12.67 ? 390  GLY A CA    1 
ATOM   2903 C C     . GLY A 1 390 ? -15.223 -14.415 30.627  1.00 12.97 ? 390  GLY A C     1 
ATOM   2904 O O     . GLY A 1 390 ? -16.358 -14.685 31.001  1.00 14.31 ? 390  GLY A O     1 
ATOM   2905 N N     . ARG A 1 391 ? -14.233 -15.292 30.615  1.00 14.17 ? 391  ARG A N     1 
ATOM   2906 C CA    . ARG A 1 391 ? -14.439 -16.670 31.029  1.00 14.58 ? 391  ARG A CA    1 
ATOM   2907 C C     . ARG A 1 391 ? -14.103 -16.796 32.509  1.00 15.25 ? 391  ARG A C     1 
ATOM   2908 O O     . ARG A 1 391 ? -13.215 -16.106 32.978  1.00 14.41 ? 391  ARG A O     1 
ATOM   2909 C CB    . ARG A 1 391 ? -13.525 -17.567 30.217  1.00 13.99 ? 391  ARG A CB    1 
ATOM   2910 C CG    . ARG A 1 391 ? -13.837 -19.047 30.327  1.00 15.89 ? 391  ARG A CG    1 
ATOM   2911 C CD    . ARG A 1 391 ? -12.816 -19.863 29.568  1.00 15.80 ? 391  ARG A CD    1 
ATOM   2912 N NE    . ARG A 1 391 ? -11.541 -19.921 30.286  1.00 17.92 ? 391  ARG A NE    1 
ATOM   2913 C CZ    . ARG A 1 391 ? -10.447 -20.570 29.903  1.00 21.20 ? 391  ARG A CZ    1 
ATOM   2914 N NH1   . ARG A 1 391 ? -10.349 -21.111 28.692  1.00 21.26 ? 391  ARG A NH1   1 
ATOM   2915 N NH2   . ARG A 1 391 ? -9.402  -20.652 30.719  1.00 21.67 ? 391  ARG A NH2   1 
ATOM   2916 N N     . THR A 1 392 ? -14.787 -17.717 33.210  1.00 15.99 ? 392  THR A N     1 
ATOM   2917 C CA    . THR A 1 392 ? -14.533 -17.952 34.634  1.00 15.80 ? 392  THR A CA    1 
ATOM   2918 C C     . THR A 1 392 ? -14.249 -19.430 34.886  1.00 17.01 ? 392  THR A C     1 
ATOM   2919 O O     . THR A 1 392 ? -14.663 -20.286 34.114  1.00 16.07 ? 392  THR A O     1 
ATOM   2920 C CB    . THR A 1 392 ? -15.695 -17.401 35.481  1.00 16.26 ? 392  THR A CB    1 
ATOM   2921 O OG1   . THR A 1 392 ? -16.893 -18.113 35.189  1.00 16.53 ? 392  THR A OG1   1 
ATOM   2922 C CG2   . THR A 1 392 ? -15.939 -15.920 35.249  1.00 16.03 ? 392  THR A CG2   1 
ATOM   2923 N N     . SER A 1 393 ? -13.496 -19.738 35.966  1.00 16.68 ? 393  SER A N     1 
ATOM   2924 C CA    . SER A 1 393 ? -13.116 -21.126 36.218  1.00 20.19 ? 393  SER A CA    1 
ATOM   2925 C C     . SER A 1 393 ? -14.291 -21.931 36.775  1.00 20.89 ? 393  SER A C     1 
ATOM   2926 O O     . SER A 1 393 ? -14.499 -23.081 36.403  1.00 27.46 ? 393  SER A O     1 
ATOM   2927 C CB    . SER A 1 393 ? -11.914 -21.218 37.138  1.00 22.15 ? 393  SER A CB    1 
ATOM   2928 O OG    . SER A 1 393 ? -12.117 -20.421 38.278  1.00 24.51 ? 393  SER A OG    1 
ATOM   2929 N N     . GLY A 1 394 ? -15.072 -21.290 37.631  1.00 21.32 ? 394  GLY A N     1 
ATOM   2930 C CA    . GLY A 1 394 ? -16.308 -21.825 38.161  1.00 19.74 ? 394  GLY A CA    1 
ATOM   2931 C C     . GLY A 1 394 ? -17.494 -20.949 37.766  1.00 18.27 ? 394  GLY A C     1 
ATOM   2932 O O     . GLY A 1 394 ? -17.446 -20.252 36.760  1.00 17.74 ? 394  GLY A O     1 
ATOM   2933 N N     . ASP A 1 395 ? -18.594 -21.047 38.504  1.00 16.53 ? 395  ASP A N     1 
ATOM   2934 C CA    . ASP A 1 395 ? -19.805 -20.336 38.145  1.00 17.81 ? 395  ASP A CA    1 
ATOM   2935 C C     . ASP A 1 395 ? -19.491 -18.848 38.015  1.00 18.61 ? 395  ASP A C     1 
ATOM   2936 O O     . ASP A 1 395 ? -18.763 -18.266 38.829  1.00 18.29 ? 395  ASP A O     1 
ATOM   2937 C CB    . ASP A 1 395 ? -20.912 -20.552 39.160  1.00 22.56 ? 395  ASP A CB    1 
ATOM   2938 C CG    . ASP A 1 395 ? -21.500 -21.956 39.196  1.00 30.15 ? 395  ASP A CG    1 
ATOM   2939 O OD1   . ASP A 1 395 ? -20.913 -22.873 38.542  1.00 32.16 ? 395  ASP A OD1   1 
ATOM   2940 O OD2   . ASP A 1 395 ? -22.551 -22.107 39.889  1.00 39.29 ? 395  ASP A OD2   1 
ATOM   2941 N N     . LEU A 1 396 ? -20.089 -18.221 36.993  1.00 17.17 ? 396  LEU A N     1 
ATOM   2942 C CA    . LEU A 1 396 ? -20.011 -16.780 36.848  1.00 16.38 ? 396  LEU A CA    1 
ATOM   2943 C C     . LEU A 1 396 ? -20.498 -16.064 38.104  1.00 17.66 ? 396  LEU A C     1 
ATOM   2944 O O     . LEU A 1 396 ? -21.540 -16.414 38.679  1.00 18.79 ? 396  LEU A O     1 
ATOM   2945 C CB    . LEU A 1 396 ? -20.925 -16.436 35.675  1.00 16.06 ? 396  LEU A CB    1 
ATOM   2946 C CG    . LEU A 1 396 ? -20.943 -14.964 35.269  1.00 16.24 ? 396  LEU A CG    1 
ATOM   2947 C CD1   . LEU A 1 396 ? -19.633 -14.603 34.613  1.00 16.80 ? 396  LEU A CD1   1 
ATOM   2948 C CD2   . LEU A 1 396 ? -22.106 -14.744 34.311  1.00 17.35 ? 396  LEU A CD2   1 
ATOM   2949 N N     . THR A 1 397 ? -19.807 -14.964 38.427  1.00 17.43 ? 397  THR A N     1 
ATOM   2950 C CA    . THR A 1 397 ? -20.183 -14.079 39.514  1.00 17.21 ? 397  THR A CA    1 
ATOM   2951 C C     . THR A 1 397 ? -20.434 -12.682 38.984  1.00 17.24 ? 397  THR A C     1 
ATOM   2952 O O     . THR A 1 397 ? -20.018 -12.312 37.879  1.00 17.88 ? 397  THR A O     1 
ATOM   2953 C CB    . THR A 1 397 ? -19.122 -14.032 40.630  1.00 17.52 ? 397  THR A CB    1 
ATOM   2954 O OG1   . THR A 1 397 ? -18.083 -13.114 40.288  1.00 19.01 ? 397  THR A OG1   1 
ATOM   2955 C CG2   . THR A 1 397 ? -18.530 -15.391 40.959  1.00 18.28 ? 397  THR A CG2   1 
ATOM   2956 N N     . ASP A 1 398 ? -21.146 -11.891 39.789  1.00 17.56 ? 398  ASP A N     1 
ATOM   2957 C CA    . ASP A 1 398 ? -21.414 -10.511 39.454  1.00 19.51 ? 398  ASP A CA    1 
ATOM   2958 C C     . ASP A 1 398 ? -20.130 -9.740  39.172  1.00 17.76 ? 398  ASP A C     1 
ATOM   2959 O O     . ASP A 1 398 ? -20.220 -8.704  38.491  1.00 17.43 ? 398  ASP A O     1 
ATOM   2960 C CB    . ASP A 1 398 ? -22.283 -9.789  40.478  1.00 23.52 ? 398  ASP A CB    1 
ATOM   2961 C CG    . ASP A 1 398 ? -22.808 -8.424  40.016  1.00 27.90 ? 398  ASP A CG    1 
ATOM   2962 O OD1   . ASP A 1 398 ? -23.354 -8.344  38.900  1.00 32.28 ? 398  ASP A OD1   1 
ATOM   2963 O OD2   . ASP A 1 398 ? -22.640 -7.421  40.746  1.00 32.30 ? 398  ASP A OD2   1 
ATOM   2964 N N     . THR A 1 399 ? -18.974 -10.159 39.731  1.00 17.10 ? 399  THR A N     1 
ATOM   2965 C CA    . THR A 1 399 ? -17.733 -9.439  39.483  1.00 17.04 ? 399  THR A CA    1 
ATOM   2966 C C     . THR A 1 399 ? -17.499 -9.351  37.970  1.00 16.30 ? 399  THR A C     1 
ATOM   2967 O O     . THR A 1 399 ? -17.152 -8.294  37.438  1.00 15.11 ? 399  THR A O     1 
ATOM   2968 C CB    . THR A 1 399 ? -16.531 -10.087 40.175  1.00 19.09 ? 399  THR A CB    1 
ATOM   2969 O OG1   . THR A 1 399 ? -16.859 -10.040 41.560  1.00 23.40 ? 399  THR A OG1   1 
ATOM   2970 C CG2   . THR A 1 399 ? -15.246 -9.302  39.945  1.00 18.62 ? 399  THR A CG2   1 
ATOM   2971 N N     . THR A 1 400 ? -17.690 -10.485 37.295  1.00 14.12 ? 400  THR A N     1 
ATOM   2972 C CA    . THR A 1 400 ? -17.389 -10.550 35.870  1.00 14.21 ? 400  THR A CA    1 
ATOM   2973 C C     . THR A 1 400 ? -18.492 -9.830  35.088  1.00 13.37 ? 400  THR A C     1 
ATOM   2974 O O     . THR A 1 400 ? -18.195 -9.186  34.093  1.00 14.95 ? 400  THR A O     1 
ATOM   2975 C CB    . THR A 1 400 ? -17.211 -11.992 35.405  1.00 13.20 ? 400  THR A CB    1 
ATOM   2976 O OG1   . THR A 1 400 ? -16.056 -12.445 36.119  1.00 14.08 ? 400  THR A OG1   1 
ATOM   2977 C CG2   . THR A 1 400 ? -16.978 -12.074 33.900  1.00 14.11 ? 400  THR A CG2   1 
ATOM   2978 N N     . VAL A 1 401 ? -19.754 -9.883  35.539  1.00 13.13 ? 401  VAL A N     1 
ATOM   2979 C CA    . VAL A 1 401 ? -20.830 -9.182  34.854  1.00 14.79 ? 401  VAL A CA    1 
ATOM   2980 C C     . VAL A 1 401 ? -20.573 -7.671  34.922  1.00 15.03 ? 401  VAL A C     1 
ATOM   2981 O O     . VAL A 1 401 ? -20.611 -6.959  33.894  1.00 13.96 ? 401  VAL A O     1 
ATOM   2982 C CB    . VAL A 1 401 ? -22.206 -9.580  35.427  1.00 15.53 ? 401  VAL A CB    1 
ATOM   2983 C CG1   . VAL A 1 401 ? -23.365 -8.806  34.797  1.00 17.83 ? 401  VAL A CG1   1 
ATOM   2984 C CG2   . VAL A 1 401 ? -22.400 -11.096 35.309  1.00 16.53 ? 401  VAL A CG2   1 
ATOM   2985 N N     . GLN A 1 402 ? -20.255 -7.166  36.127  1.00 16.85 ? 402  GLN A N     1 
ATOM   2986 C CA    . GLN A 1 402 ? -19.939 -5.754  36.256  1.00 18.51 ? 402  GLN A CA    1 
ATOM   2987 C C     . GLN A 1 402 ? -18.714 -5.382  35.418  1.00 15.38 ? 402  GLN A C     1 
ATOM   2988 O O     . GLN A 1 402 ? -18.650 -4.279  34.864  1.00 15.32 ? 402  GLN A O     1 
ATOM   2989 C CB    . GLN A 1 402 ? -19.832 -5.377  37.739  1.00 23.10 ? 402  GLN A CB    1 
ATOM   2990 C CG    . GLN A 1 402 ? -21.217 -5.130  38.330  1.00 29.71 ? 402  GLN A CG    1 
ATOM   2991 C CD    . GLN A 1 402 ? -22.096 -4.328  37.366  1.00 40.76 ? 402  GLN A CD    1 
ATOM   2992 O OE1   . GLN A 1 402 ? -21.880 -3.123  37.145  1.00 42.30 ? 402  GLN A OE1   1 
ATOM   2993 N NE2   . GLN A 1 402 ? -23.053 -4.992  36.704  1.00 37.46 ? 402  GLN A NE2   1 
ATOM   2994 N N     . PHE A 1 403 ? -17.725 -6.263  35.393  1.00 14.48 ? 403  PHE A N     1 
ATOM   2995 C CA    . PHE A 1 403 ? -16.529 -6.049  34.592  1.00 14.56 ? 403  PHE A CA    1 
ATOM   2996 C C     . PHE A 1 403 ? -16.885 -5.709  33.140  1.00 14.65 ? 403  PHE A C     1 
ATOM   2997 O O     . PHE A 1 403 ? -16.490 -4.655  32.611  1.00 13.23 ? 403  PHE A O     1 
ATOM   2998 C CB    . PHE A 1 403 ? -15.620 -7.274  34.675  1.00 14.82 ? 403  PHE A CB    1 
ATOM   2999 C CG    . PHE A 1 403 ? -14.413 -7.215  33.761  1.00 13.45 ? 403  PHE A CG    1 
ATOM   3000 C CD1   . PHE A 1 403 ? -13.507 -6.170  33.838  1.00 14.33 ? 403  PHE A CD1   1 
ATOM   3001 C CD2   . PHE A 1 403 ? -14.191 -8.220  32.828  1.00 14.53 ? 403  PHE A CD2   1 
ATOM   3002 C CE1   . PHE A 1 403 ? -12.384 -6.151  33.027  1.00 14.34 ? 403  PHE A CE1   1 
ATOM   3003 C CE2   . PHE A 1 403 ? -13.097 -8.170  31.976  1.00 14.88 ? 403  PHE A CE2   1 
ATOM   3004 C CZ    . PHE A 1 403 ? -12.199 -7.139  32.093  1.00 15.43 ? 403  PHE A CZ    1 
ATOM   3005 N N     . LEU A 1 404 ? -17.651 -6.604  32.479  1.00 14.74 ? 404  LEU A N     1 
ATOM   3006 C CA    . LEU A 1 404 ? -17.994 -6.384  31.077  1.00 13.77 ? 404  LEU A CA    1 
ATOM   3007 C C     . LEU A 1 404 ? -18.973 -5.224  30.898  1.00 13.32 ? 404  LEU A C     1 
ATOM   3008 O O     . LEU A 1 404 ? -18.874 -4.458  29.929  1.00 13.70 ? 404  LEU A O     1 
ATOM   3009 C CB    . LEU A 1 404 ? -18.500 -7.662  30.411  1.00 13.73 ? 404  LEU A CB    1 
ATOM   3010 C CG    . LEU A 1 404 ? -17.446 -8.764  30.334  1.00 13.74 ? 404  LEU A CG    1 
ATOM   3011 C CD1   . LEU A 1 404 ? -18.012 -9.919  29.570  1.00 14.21 ? 404  LEU A CD1   1 
ATOM   3012 C CD2   . LEU A 1 404 ? -16.116 -8.283  29.777  1.00 15.17 ? 404  LEU A CD2   1 
ATOM   3013 N N     . ASP A 1 405 ? -19.918 -5.075  31.823  1.00 13.32 ? 405  ASP A N     1 
ATOM   3014 C CA    . ASP A 1 405 ? -20.849 -3.962  31.751  1.00 14.70 ? 405  ASP A CA    1 
ATOM   3015 C C     . ASP A 1 405 ? -20.099 -2.642  31.788  1.00 14.25 ? 405  ASP A C     1 
ATOM   3016 O O     . ASP A 1 405 ? -20.352 -1.739  30.989  1.00 15.10 ? 405  ASP A O     1 
ATOM   3017 C CB    . ASP A 1 405 ? -21.863 -4.027  32.884  1.00 15.12 ? 405  ASP A CB    1 
ATOM   3018 C CG    . ASP A 1 405 ? -22.997 -5.021  32.686  1.00 17.73 ? 405  ASP A CG    1 
ATOM   3019 O OD1   . ASP A 1 405 ? -23.100 -5.588  31.572  1.00 19.15 ? 405  ASP A OD1   1 
ATOM   3020 O OD2   . ASP A 1 405 ? -23.789 -5.213  33.643  1.00 16.61 ? 405  ASP A OD2   1 
ATOM   3021 N N     . GLY A 1 406 ? -19.186 -2.507  32.748  1.00 14.38 ? 406  GLY A N     1 
ATOM   3022 C CA    . GLY A 1 406 ? -18.434 -1.266  32.864  1.00 14.11 ? 406  GLY A CA    1 
ATOM   3023 C C     . GLY A 1 406 ? -17.502 -1.048  31.664  1.00 14.14 ? 406  GLY A C     1 
ATOM   3024 O O     . GLY A 1 406 ? -17.159 0.081   31.310  1.00 14.94 ? 406  GLY A O     1 
ATOM   3025 N N     . LEU A 1 407 ? -17.064 -2.133  31.038  1.00 13.65 ? 407  LEU A N     1 
ATOM   3026 C CA    . LEU A 1 407 ? -16.214 -2.034  29.865  1.00 13.15 ? 407  LEU A CA    1 
ATOM   3027 C C     . LEU A 1 407 ? -17.004 -1.418  28.700  1.00 13.98 ? 407  LEU A C     1 
ATOM   3028 O O     . LEU A 1 407 ? -16.481 -0.579  27.971  1.00 13.61 ? 407  LEU A O     1 
ATOM   3029 C CB    . LEU A 1 407 ? -15.664 -3.415  29.504  1.00 13.41 ? 407  LEU A CB    1 
ATOM   3030 C CG    . LEU A 1 407 ? -14.814 -3.468  28.228  1.00 14.50 ? 407  LEU A CG    1 
ATOM   3031 C CD1   . LEU A 1 407 ? -13.560 -2.632  28.313  1.00 15.33 ? 407  LEU A CD1   1 
ATOM   3032 C CD2   . LEU A 1 407 ? -14.451 -4.931  27.907  1.00 14.65 ? 407  LEU A CD2   1 
ATOM   3033 N N     . SER A 1 408 ? -18.240 -1.881  28.505  1.00 13.93 ? 408  SER A N     1 
ATOM   3034 C CA    . SER A 1 408 ? -19.056 -1.328  27.442  1.00 14.14 ? 408  SER A CA    1 
ATOM   3035 C C     . SER A 1 408 ? -19.315 0.162   27.677  1.00 13.41 ? 408  SER A C     1 
ATOM   3036 O O     . SER A 1 408 ? -19.387 0.942   26.744  1.00 13.98 ? 408  SER A O     1 
ATOM   3037 C CB    . SER A 1 408 ? -20.331 -2.113  27.254  1.00 13.77 ? 408  SER A CB    1 
ATOM   3038 O OG    . SER A 1 408 ? -20.095 -3.336  26.569  1.00 13.36 ? 408  SER A OG    1 
ATOM   3039 N N     . GLU A 1 409 ? -19.502 0.555   28.922  1.00 14.75 ? 409  GLU A N     1 
ATOM   3040 C CA    . GLU A 1 409 ? -19.743 1.949   29.270  1.00 16.74 ? 409  GLU A CA    1 
ATOM   3041 C C     . GLU A 1 409 ? -18.526 2.794   28.911  1.00 16.44 ? 409  GLU A C     1 
ATOM   3042 O O     . GLU A 1 409 ? -18.665 3.843   28.290  1.00 15.74 ? 409  GLU A O     1 
ATOM   3043 C CB    . GLU A 1 409 ? -20.166 2.074   30.733  1.00 20.21 ? 409  GLU A CB    1 
ATOM   3044 C CG    . GLU A 1 409 ? -21.540 1.483   31.016  1.00 27.82 ? 409  GLU A CG    1 
ATOM   3045 C CD    . GLU A 1 409 ? -21.914 1.575   32.490  1.00 38.03 ? 409  GLU A CD    1 
ATOM   3046 O OE1   . GLU A 1 409 ? -21.137 2.201   33.256  1.00 42.71 ? 409  GLU A OE1   1 
ATOM   3047 O OE2   . GLU A 1 409 ? -22.986 1.045   32.870  1.00 45.08 ? 409  GLU A OE2   1 
ATOM   3048 N N     . VAL A 1 410 ? -17.325 2.355   29.300  1.00 16.01 ? 410  VAL A N     1 
ATOM   3049 C CA    . VAL A 1 410 ? -16.139 3.159   29.014  1.00 16.43 ? 410  VAL A CA    1 
ATOM   3050 C C     . VAL A 1 410 ? -15.871 3.155   27.497  1.00 15.85 ? 410  VAL A C     1 
ATOM   3051 O O     . VAL A 1 410 ? -15.476 4.170   26.931  1.00 15.10 ? 410  VAL A O     1 
ATOM   3052 C CB    . VAL A 1 410 ? -14.907 2.778   29.871  1.00 16.95 ? 410  VAL A CB    1 
ATOM   3053 C CG1   . VAL A 1 410 ? -14.394 1.362   29.648  1.00 18.52 ? 410  VAL A CG1   1 
ATOM   3054 C CG2   . VAL A 1 410 ? -13.740 3.730   29.661  1.00 17.65 ? 410  VAL A CG2   1 
ATOM   3055 N N     . LEU A 1 411 ? -16.150 2.037   26.794  1.00 14.13 ? 411  LEU A N     1 
ATOM   3056 C CA    . LEU A 1 411 ? -15.924 1.992   25.352  1.00 13.90 ? 411  LEU A CA    1 
ATOM   3057 C C     . LEU A 1 411 ? -16.776 3.029   24.630  1.00 13.55 ? 411  LEU A C     1 
ATOM   3058 O O     . LEU A 1 411 ? -16.349 3.472   23.583  1.00 14.94 ? 411  LEU A O     1 
ATOM   3059 C CB    . LEU A 1 411 ? -16.212 0.604   24.797  1.00 14.15 ? 411  LEU A CB    1 
ATOM   3060 C CG    . LEU A 1 411 ? -15.138 -0.453  25.035  1.00 12.71 ? 411  LEU A CG    1 
ATOM   3061 C CD1   . LEU A 1 411 ? -15.692 -1.881  24.866  1.00 14.50 ? 411  LEU A CD1   1 
ATOM   3062 C CD2   . LEU A 1 411 ? -13.997 -0.259  24.082  1.00 12.42 ? 411  LEU A CD2   1 
ATOM   3063 N N     . THR A 1 412 ? -17.979 3.330   25.147  1.00 13.61 ? 412  THR A N     1 
ATOM   3064 C CA    . THR A 1 412 ? -18.911 4.246   24.511  1.00 15.29 ? 412  THR A CA    1 
ATOM   3065 C C     . THR A 1 412 ? -18.840 5.643   25.127  1.00 16.24 ? 412  THR A C     1 
ATOM   3066 O O     . THR A 1 412 ? -19.607 6.522   24.718  1.00 15.94 ? 412  THR A O     1 
ATOM   3067 C CB    . THR A 1 412 ? -20.340 3.718   24.588  1.00 17.39 ? 412  THR A CB    1 
ATOM   3068 O OG1   . THR A 1 412 ? -20.696 3.443   25.941  1.00 16.53 ? 412  THR A OG1   1 
ATOM   3069 C CG2   . THR A 1 412 ? -20.496 2.452   23.758  1.00 18.60 ? 412  THR A CG2   1 
ATOM   3070 N N     . SER A 1 413 ? -17.910 5.841   26.054  1.00 14.51 ? 413  SER A N     1 
ATOM   3071 C CA    . SER A 1 413 ? -17.878 7.058   26.853  1.00 16.13 ? 413  SER A CA    1 
ATOM   3072 C C     . SER A 1 413 ? -17.537 8.316   26.034  1.00 16.79 ? 413  SER A C     1 
ATOM   3073 O O     . SER A 1 413 ? -17.805 9.438   26.480  1.00 18.59 ? 413  SER A O     1 
ATOM   3074 C CB    . SER A 1 413 ? -16.943 6.871   28.040  1.00 16.41 ? 413  SER A CB    1 
ATOM   3075 O OG    . SER A 1 413 ? -15.583 6.721   27.652  1.00 17.81 ? 413  SER A OG    1 
ATOM   3076 N N     . GLY A 1 414 ? -16.926 8.158   24.859  1.00 17.99 ? 414  GLY A N     1 
ATOM   3077 C CA    . GLY A 1 414 ? -16.678 9.310   24.007  1.00 19.00 ? 414  GLY A CA    1 
ATOM   3078 C C     . GLY A 1 414 ? -17.956 9.961   23.490  1.00 19.18 ? 414  GLY A C     1 
ATOM   3079 O O     . GLY A 1 414 ? -17.939 11.143  23.117  1.00 21.19 ? 414  GLY A O     1 
ATOM   3080 N N     . GLN A 1 415 ? -19.042 9.171   23.388  1.00 18.21 ? 415  GLN A N     1 
ATOM   3081 C CA    . GLN A 1 415 ? -20.330 9.636   22.889  1.00 20.50 ? 415  GLN A CA    1 
ATOM   3082 C C     . GLN A 1 415 ? -21.419 8.770   23.507  1.00 20.69 ? 415  GLN A C     1 
ATOM   3083 O O     . GLN A 1 415 ? -21.936 7.819   22.905  1.00 19.56 ? 415  GLN A O     1 
ATOM   3084 C CB    . GLN A 1 415 ? -20.449 9.516   21.381  1.00 20.01 ? 415  GLN A CB    1 
ATOM   3085 C CG    . GLN A 1 415 ? -20.150 10.764  20.588  1.00 21.08 ? 415  GLN A CG    1 
ATOM   3086 C CD    . GLN A 1 415 ? -20.348 10.501  19.111  1.00 18.98 ? 415  GLN A CD    1 
ATOM   3087 O OE1   . GLN A 1 415 ? -19.428 10.062  18.401  1.00 20.30 ? 415  GLN A OE1   1 
ATOM   3088 N NE2   . GLN A 1 415 ? -21.544 10.799  18.644  1.00 17.79 ? 415  GLN A NE2   1 
ATOM   3089 N N     . PRO A 1 416 ? -21.701 8.964   24.808  1.00 19.53 ? 416  PRO A N     1 
ATOM   3090 C CA    . PRO A 1 416 ? -22.539 8.006   25.530  1.00 20.57 ? 416  PRO A CA    1 
ATOM   3091 C C     . PRO A 1 416 ? -23.972 7.855   25.022  1.00 20.16 ? 416  PRO A C     1 
ATOM   3092 O O     . PRO A 1 416 ? -24.566 6.819   25.243  1.00 22.45 ? 416  PRO A O     1 
ATOM   3093 C CB    . PRO A 1 416 ? -22.495 8.455   26.973  1.00 22.43 ? 416  PRO A CB    1 
ATOM   3094 C CG    . PRO A 1 416 ? -21.880 9.839   26.955  1.00 21.44 ? 416  PRO A CG    1 
ATOM   3095 C CD    . PRO A 1 416 ? -21.175 10.070  25.632  1.00 20.68 ? 416  PRO A CD    1 
ATOM   3096 N N     . ASP A 1 417 ? -24.503 8.860   24.330  1.00 21.40 ? 417  ASP A N     1 
ATOM   3097 C CA    . ASP A 1 417 ? -25.906 8.833   23.936  1.00 24.99 ? 417  ASP A CA    1 
ATOM   3098 C C     . ASP A 1 417 ? -26.086 8.525   22.454  1.00 22.82 ? 417  ASP A C     1 
ATOM   3099 O O     . ASP A 1 417 ? -27.211 8.582   21.956  1.00 23.63 ? 417  ASP A O     1 
ATOM   3100 C CB    . ASP A 1 417 ? -26.603 10.137  24.283  1.00 28.76 ? 417  ASP A CB    1 
ATOM   3101 C CG    . ASP A 1 417 ? -26.518 10.523  25.748  1.00 32.36 ? 417  ASP A CG    1 
ATOM   3102 O OD1   . ASP A 1 417 ? -26.734 9.639   26.589  1.00 35.23 ? 417  ASP A OD1   1 
ATOM   3103 O OD2   . ASP A 1 417 ? -26.227 11.702  26.021  1.00 38.67 ? 417  ASP A OD2   1 
ATOM   3104 N N     . ALA A 1 418 ? -25.000 8.218   21.733  1.00 20.89 ? 418  ALA A N     1 
ATOM   3105 C CA    . ALA A 1 418 ? -25.099 7.800   20.343  1.00 19.76 ? 418  ALA A CA    1 
ATOM   3106 C C     . ALA A 1 418 ? -25.701 6.402   20.228  1.00 19.61 ? 418  ALA A C     1 
ATOM   3107 O O     . ALA A 1 418 ? -25.758 5.634   21.190  1.00 19.66 ? 418  ALA A O     1 
ATOM   3108 C CB    . ALA A 1 418 ? -23.736 7.824   19.702  1.00 21.00 ? 418  ALA A CB    1 
ATOM   3109 N N     . TYR A 1 419 ? -26.137 6.068   19.002  1.00 16.89 ? 419  TYR A N     1 
ATOM   3110 C CA    . TYR A 1 419 ? -26.616 4.731   18.735  1.00 15.82 ? 419  TYR A CA    1 
ATOM   3111 C C     . TYR A 1 419 ? -25.423 3.788   18.640  1.00 15.44 ? 419  TYR A C     1 
ATOM   3112 O O     . TYR A 1 419 ? -24.491 4.020   17.867  1.00 15.99 ? 419  TYR A O     1 
ATOM   3113 C CB    . TYR A 1 419 ? -27.463 4.648   17.463  1.00 15.75 ? 419  TYR A CB    1 
ATOM   3114 C CG    . TYR A 1 419 ? -27.839 3.209   17.170  1.00 14.06 ? 419  TYR A CG    1 
ATOM   3115 C CD1   . TYR A 1 419 ? -28.802 2.554   17.928  1.00 14.76 ? 419  TYR A CD1   1 
ATOM   3116 C CD2   . TYR A 1 419 ? -27.172 2.473   16.209  1.00 13.98 ? 419  TYR A CD2   1 
ATOM   3117 C CE1   . TYR A 1 419 ? -29.161 1.242   17.666  1.00 15.01 ? 419  TYR A CE1   1 
ATOM   3118 C CE2   . TYR A 1 419 ? -27.520 1.158   15.940  1.00 14.52 ? 419  TYR A CE2   1 
ATOM   3119 C CZ    . TYR A 1 419 ? -28.488 0.523   16.705  1.00 13.97 ? 419  TYR A CZ    1 
ATOM   3120 O OH    . TYR A 1 419 ? -28.865 -0.763  16.461  1.00 14.91 ? 419  TYR A OH    1 
ATOM   3121 N N     . TYR A 1 420 ? -25.513 2.671   19.368  1.00 14.60 ? 420  TYR A N     1 
ATOM   3122 C CA    . TYR A 1 420 ? -24.542 1.587   19.258  1.00 15.27 ? 420  TYR A CA    1 
ATOM   3123 C C     . TYR A 1 420 ? -25.277 0.282   19.010  1.00 13.58 ? 420  TYR A C     1 
ATOM   3124 O O     . TYR A 1 420 ? -26.087 -0.171  19.823  1.00 14.36 ? 420  TYR A O     1 
ATOM   3125 C CB    . TYR A 1 420 ? -23.624 1.393   20.475  1.00 15.25 ? 420  TYR A CB    1 
ATOM   3126 C CG    . TYR A 1 420 ? -22.780 2.623   20.750  1.00 15.48 ? 420  TYR A CG    1 
ATOM   3127 C CD1   . TYR A 1 420 ? -21.546 2.810   20.144  1.00 14.05 ? 420  TYR A CD1   1 
ATOM   3128 C CD2   . TYR A 1 420 ? -23.277 3.638   21.574  1.00 14.92 ? 420  TYR A CD2   1 
ATOM   3129 C CE1   . TYR A 1 420 ? -20.801 3.955   20.354  1.00 15.03 ? 420  TYR A CE1   1 
ATOM   3130 C CE2   . TYR A 1 420 ? -22.564 4.811   21.743  1.00 15.89 ? 420  TYR A CE2   1 
ATOM   3131 C CZ    . TYR A 1 420 ? -21.313 4.954   21.165  1.00 14.37 ? 420  TYR A CZ    1 
ATOM   3132 O OH    . TYR A 1 420 ? -20.565 6.077   21.369  1.00 16.52 ? 420  TYR A OH    1 
ATOM   3133 N N     . GLY A 1 421 ? -25.002 -0.306  17.872  1.00 12.37 ? 421  GLY A N     1 
ATOM   3134 C CA    . GLY A 1 421 ? -25.508 -1.626  17.568  1.00 13.13 ? 421  GLY A CA    1 
ATOM   3135 C C     . GLY A 1 421 ? -24.880 -2.711  18.429  1.00 13.12 ? 421  GLY A C     1 
ATOM   3136 O O     . GLY A 1 421 ? -23.891 -2.497  19.143  1.00 12.19 ? 421  GLY A O     1 
ATOM   3137 N N     . GLN A 1 422 ? -25.529 -3.868  18.361  1.00 13.71 ? 422  GLN A N     1 
ATOM   3138 C CA    . GLN A 1 422 ? -25.013 -5.098  18.940  1.00 12.41 ? 422  GLN A CA    1 
ATOM   3139 C C     . GLN A 1 422 ? -25.253 -6.203  17.922  1.00 13.45 ? 422  GLN A C     1 
ATOM   3140 O O     . GLN A 1 422 ? -26.241 -6.154  17.187  1.00 13.19 ? 422  GLN A O     1 
ATOM   3141 C CB    . GLN A 1 422 ? -25.780 -5.450  20.210  1.00 12.44 ? 422  GLN A CB    1 
ATOM   3142 C CG    . GLN A 1 422 ? -25.521 -4.493  21.375  1.00 12.81 ? 422  GLN A CG    1 
ATOM   3143 C CD    . GLN A 1 422 ? -26.199 -4.922  22.660  1.00 13.60 ? 422  GLN A CD    1 
ATOM   3144 O OE1   . GLN A 1 422 ? -26.169 -6.100  23.042  1.00 13.75 ? 422  GLN A OE1   1 
ATOM   3145 N NE2   . GLN A 1 422 ? -26.940 -4.010  23.250  1.00 15.58 ? 422  GLN A NE2   1 
ATOM   3146 N N     . TYR A 1 423 ? -24.355 -7.181  17.894  1.00 13.12 ? 423  TYR A N     1 
ATOM   3147 C CA    . TYR A 1 423 ? -24.504 -8.306  16.990  1.00 12.34 ? 423  TYR A CA    1 
ATOM   3148 C C     . TYR A 1 423 ? -25.368 -9.386  17.629  1.00 13.35 ? 423  TYR A C     1 
ATOM   3149 O O     . TYR A 1 423 ? -24.985 -9.967  18.641  1.00 14.70 ? 423  TYR A O     1 
ATOM   3150 C CB    . TYR A 1 423 ? -23.145 -8.904  16.643  1.00 12.68 ? 423  TYR A CB    1 
ATOM   3151 C CG    . TYR A 1 423 ? -23.137 -10.014 15.583  1.00 11.58 ? 423  TYR A CG    1 
ATOM   3152 C CD1   . TYR A 1 423 ? -24.009 -10.009 14.494  1.00 12.50 ? 423  TYR A CD1   1 
ATOM   3153 C CD2   . TYR A 1 423 ? -22.292 -11.093 15.700  1.00 12.43 ? 423  TYR A CD2   1 
ATOM   3154 C CE1   . TYR A 1 423 ? -23.960 -10.988 13.512  1.00 12.73 ? 423  TYR A CE1   1 
ATOM   3155 C CE2   . TYR A 1 423 ? -22.214 -12.066 14.721  1.00 12.29 ? 423  TYR A CE2   1 
ATOM   3156 C CZ    . TYR A 1 423 ? -23.032 -12.002 13.605  1.00 11.76 ? 423  TYR A CZ    1 
ATOM   3157 O OH    . TYR A 1 423 ? -22.983 -12.959 12.631  1.00 11.95 ? 423  TYR A OH    1 
ATOM   3158 N N     . VAL A 1 424 ? -26.506 -9.688  16.980  1.00 12.12 ? 424  VAL A N     1 
ATOM   3159 C CA    . VAL A 1 424 ? -27.451 -10.637 17.513  1.00 12.35 ? 424  VAL A CA    1 
ATOM   3160 C C     . VAL A 1 424 ? -26.873 -12.047 17.424  1.00 11.61 ? 424  VAL A C     1 
ATOM   3161 O O     . VAL A 1 424 ? -27.405 -12.976 18.021  1.00 12.12 ? 424  VAL A O     1 
ATOM   3162 C CB    . VAL A 1 424 ? -28.821 -10.504 16.813  1.00 11.96 ? 424  VAL A CB    1 
ATOM   3163 C CG1   . VAL A 1 424 ? -28.774 -11.011 15.381  1.00 12.83 ? 424  VAL A CG1   1 
ATOM   3164 C CG2   . VAL A 1 424 ? -29.908 -11.214 17.596  1.00 14.13 ? 424  VAL A CG2   1 
ATOM   3165 N N     . GLY A 1 425 ? -25.753 -12.217 16.703  1.00 12.79 ? 425  GLY A N     1 
ATOM   3166 C CA    . GLY A 1 425 ? -25.024 -13.479 16.690  1.00 12.65 ? 425  GLY A CA    1 
ATOM   3167 C C     . GLY A 1 425 ? -24.297 -13.760 18.008  1.00 13.23 ? 425  GLY A C     1 
ATOM   3168 O O     . GLY A 1 425 ? -23.916 -14.904 18.288  1.00 13.53 ? 425  GLY A O     1 
ATOM   3169 N N     . ASN A 1 426 ? -24.101 -12.699 18.810  1.00 12.40 ? 426  ASN A N     1 
ATOM   3170 C CA    . ASN A 1 426 ? -23.523 -12.844 20.143  1.00 16.15 ? 426  ASN A CA    1 
ATOM   3171 C C     . ASN A 1 426 ? -24.494 -12.234 21.154  1.00 14.02 ? 426  ASN A C     1 
ATOM   3172 O O     . ASN A 1 426 ? -24.334 -11.092 21.614  1.00 13.56 ? 426  ASN A O     1 
ATOM   3173 C CB    . ASN A 1 426 ? -22.108 -12.298 20.167  1.00 19.68 ? 426  ASN A CB    1 
ATOM   3174 C CG    . ASN A 1 426 ? -21.107 -13.161 19.392  1.00 26.99 ? 426  ASN A CG    1 
ATOM   3175 O OD1   . ASN A 1 426 ? -21.058 -14.414 19.476  1.00 27.01 ? 426  ASN A OD1   1 
ATOM   3176 N ND2   . ASN A 1 426 ? -20.217 -12.491 18.682  1.00 33.38 ? 426  ASN A ND2   1 
ATOM   3177 N N     . VAL A 1 427 ? -25.510 -13.010 21.523  1.00 12.53 ? 427  VAL A N     1 
ATOM   3178 C CA    . VAL A 1 427 ? -26.569 -12.483 22.371  1.00 12.50 ? 427  VAL A CA    1 
ATOM   3179 C C     . VAL A 1 427 ? -25.995 -12.163 23.740  1.00 11.51 ? 427  VAL A C     1 
ATOM   3180 O O     . VAL A 1 427 ? -25.061 -12.808 24.217  1.00 12.10 ? 427  VAL A O     1 
ATOM   3181 C CB    . VAL A 1 427 ? -27.812 -13.382 22.487  1.00 12.76 ? 427  VAL A CB    1 
ATOM   3182 C CG1   . VAL A 1 427 ? -28.469 -13.589 21.098  1.00 13.00 ? 427  VAL A CG1   1 
ATOM   3183 C CG2   . VAL A 1 427 ? -27.508 -14.700 23.187  1.00 11.82 ? 427  VAL A CG2   1 
ATOM   3184 N N     . ASP A 1 428 ? -26.529 -11.081 24.305  1.00 11.80 ? 428  ASP A N     1 
ATOM   3185 C CA    . ASP A 1 428 ? -26.211 -10.647 25.651  1.00 12.22 ? 428  ASP A CA    1 
ATOM   3186 C C     . ASP A 1 428 ? -27.495 -10.697 26.469  1.00 11.85 ? 428  ASP A C     1 
ATOM   3187 O O     . ASP A 1 428 ? -28.320 -9.801  26.374  1.00 13.32 ? 428  ASP A O     1 
ATOM   3188 C CB    . ASP A 1 428 ? -25.646 -9.238  25.617  1.00 12.51 ? 428  ASP A CB    1 
ATOM   3189 C CG    . ASP A 1 428 ? -25.387 -8.615  26.975  1.00 13.79 ? 428  ASP A CG    1 
ATOM   3190 O OD1   . ASP A 1 428 ? -25.705 -9.285  28.010  1.00 13.44 ? 428  ASP A OD1   1 
ATOM   3191 O OD2   . ASP A 1 428 ? -24.904 -7.497  26.977  1.00 13.48 ? 428  ASP A OD2   1 
ATOM   3192 N N     . PRO A 1 429 ? -27.738 -11.780 27.221  1.00 12.35 ? 429  PRO A N     1 
ATOM   3193 C CA    . PRO A 1 429 ? -28.982 -11.905 27.995  1.00 12.24 ? 429  PRO A CA    1 
ATOM   3194 C C     . PRO A 1 429 ? -29.050 -11.038 29.244  1.00 12.81 ? 429  PRO A C     1 
ATOM   3195 O O     . PRO A 1 429 ? -30.109 -10.987 29.853  1.00 14.92 ? 429  PRO A O     1 
ATOM   3196 C CB    . PRO A 1 429 ? -29.039 -13.384 28.398  1.00 12.42 ? 429  PRO A CB    1 
ATOM   3197 C CG    . PRO A 1 429 ? -27.932 -14.033 27.627  1.00 13.97 ? 429  PRO A CG    1 
ATOM   3198 C CD    . PRO A 1 429 ? -26.911 -12.977 27.299  1.00 12.90 ? 429  PRO A CD    1 
ATOM   3199 N N     . ARG A 1 430 ? -27.950 -10.392 29.621  1.00 12.75 ? 430  ARG A N     1 
ATOM   3200 C CA    . ARG A 1 430 ? -27.922 -9.623  30.894  1.00 12.44 ? 430  ARG A CA    1 
ATOM   3201 C C     . ARG A 1 430 ? -28.120 -8.129  30.623  1.00 13.61 ? 430  ARG A C     1 
ATOM   3202 O O     . ARG A 1 430 ? -27.281 -7.334  31.045  1.00 15.72 ? 430  ARG A O     1 
ATOM   3203 C CB    . ARG A 1 430 ? -26.627 -9.934  31.649  1.00 11.82 ? 430  ARG A CB    1 
ATOM   3204 C CG    . ARG A 1 430 ? -26.425 -11.429 31.838  1.00 11.98 ? 430  ARG A CG    1 
ATOM   3205 C CD    . ARG A 1 430 ? -25.237 -11.732 32.729  1.00 12.58 ? 430  ARG A CD    1 
ATOM   3206 N NE    . ARG A 1 430 ? -24.885 -13.154 32.703  1.00 13.44 ? 430  ARG A NE    1 
ATOM   3207 C CZ    . ARG A 1 430 ? -25.438 -14.071 33.477  1.00 16.56 ? 430  ARG A CZ    1 
ATOM   3208 N NH1   . ARG A 1 430 ? -26.161 -13.709 34.519  1.00 16.86 ? 430  ARG A NH1   1 
ATOM   3209 N NH2   . ARG A 1 430 ? -25.253 -15.348 33.215  1.00 15.68 ? 430  ARG A NH2   1 
ATOM   3210 N N     . GLN A 1 431 ? -29.211 -7.814  29.948  1.00 14.75 ? 431  GLN A N     1 
ATOM   3211 C CA    . GLN A 1 431 ? -29.554 -6.411  29.652  1.00 15.12 ? 431  GLN A CA    1 
ATOM   3212 C C     . GLN A 1 431 ? -31.066 -6.337  29.414  1.00 15.22 ? 431  GLN A C     1 
ATOM   3213 O O     . GLN A 1 431 ? -31.676 -7.397  29.254  1.00 16.18 ? 431  GLN A O     1 
ATOM   3214 C CB    . GLN A 1 431 ? -28.793 -5.928  28.418  1.00 15.04 ? 431  GLN A CB    1 
ATOM   3215 C CG    . GLN A 1 431 ? -29.195 -6.600  27.114  1.00 14.61 ? 431  GLN A CG    1 
ATOM   3216 C CD    . GLN A 1 431 ? -28.392 -6.106  25.933  1.00 15.82 ? 431  GLN A CD    1 
ATOM   3217 O OE1   . GLN A 1 431 ? -28.015 -4.935  25.862  1.00 17.25 ? 431  GLN A OE1   1 
ATOM   3218 N NE2   . GLN A 1 431 ? -28.118 -7.000  24.997  1.00 15.50 ? 431  GLN A NE2   1 
ATOM   3219 N N     . PRO A 1 432 ? -31.672 -5.136  29.418  1.00 15.27 ? 432  PRO A N     1 
ATOM   3220 C CA    . PRO A 1 432 ? -33.073 -4.978  29.091  1.00 17.50 ? 432  PRO A CA    1 
ATOM   3221 C C     . PRO A 1 432 ? -33.331 -5.562  27.723  1.00 18.15 ? 432  PRO A C     1 
ATOM   3222 O O     . PRO A 1 432 ? -32.496 -5.431  26.842  1.00 16.45 ? 432  PRO A O     1 
ATOM   3223 C CB    . PRO A 1 432 ? -33.317 -3.445  29.019  1.00 30.00 ? 432  PRO A CB    1 
ATOM   3224 C CG    . PRO A 1 432 ? -32.227 -2.889  29.895  1.00 30.00 ? 432  PRO A CG    1 
ATOM   3225 C CD    . PRO A 1 432 ? -31.061 -3.868  29.793  1.00 30.00 ? 432  PRO A CD    1 
ATOM   3226 N N     . THR A 1 433 ? -34.525 -6.103  27.556  1.00 16.86 ? 433  THR A N     1 
ATOM   3227 C CA    . THR A 1 433 ? -34.904 -6.631  26.240  1.00 17.22 ? 433  THR A CA    1 
ATOM   3228 C C     . THR A 1 433 ? -35.067 -5.477  25.260  1.00 18.09 ? 433  THR A C     1 
ATOM   3229 O O     . THR A 1 433 ? -34.743 -5.635  24.097  1.00 15.64 ? 433  THR A O     1 
ATOM   3230 C CB    . THR A 1 433 ? -36.160 -7.487  26.423  1.00 17.99 ? 433  THR A CB    1 
ATOM   3231 O OG1   . THR A 1 433 ? -35.791 -8.524  27.323  1.00 21.43 ? 433  THR A OG1   1 
ATOM   3232 C CG2   . THR A 1 433 ? -36.653 -8.080  25.117  1.00 17.77 ? 433  THR A CG2   1 
ATOM   3233 N N     . ASP A 1 434 ? -35.500 -4.330  25.773  1.00 18.19 ? 434  ASP A N     1 
ATOM   3234 C CA    . ASP A 1 434 ? -35.661 -3.131  24.909  1.00 21.92 ? 434  ASP A CA    1 
ATOM   3235 C C     . ASP A 1 434 ? -34.305 -2.718  24.335  1.00 18.31 ? 434  ASP A C     1 
ATOM   3236 O O     . ASP A 1 434 ? -34.226 -2.399  23.153  1.00 18.14 ? 434  ASP A O     1 
ATOM   3237 C CB    . ASP A 1 434 ? -36.315 -1.982  25.658  1.00 28.52 ? 434  ASP A CB    1 
ATOM   3238 C CG    . ASP A 1 434 ? -37.807 -2.152  25.893  1.00 37.89 ? 434  ASP A CG    1 
ATOM   3239 O OD1   . ASP A 1 434 ? -38.394 -3.059  25.275  1.00 39.47 ? 434  ASP A OD1   1 
ATOM   3240 O OD2   . ASP A 1 434 ? -38.364 -1.385  26.699  1.00 48.32 ? 434  ASP A OD2   1 
ATOM   3241 N N     . GLU A 1 435 ? -33.296 -2.685  25.193  1.00 17.86 ? 435  GLU A N     1 
ATOM   3242 C CA    . GLU A 1 435 ? -31.951 -2.264  24.744  1.00 18.02 ? 435  GLU A CA    1 
ATOM   3243 C C     . GLU A 1 435 ? -31.405 -3.305  23.765  1.00 16.39 ? 435  GLU A C     1 
ATOM   3244 O O     . GLU A 1 435 ? -30.796 -2.929  22.780  1.00 16.66 ? 435  GLU A O     1 
ATOM   3245 C CB    . GLU A 1 435 ? -31.008 -2.096  25.931  1.00 30.00 ? 435  GLU A CB    1 
ATOM   3246 C CG    . GLU A 1 435 ? -29.578 -1.784  25.504  1.00 30.00 ? 435  GLU A CG    1 
ATOM   3247 C CD    . GLU A 1 435 ? -28.657 -1.392  26.637  1.00 30.00 ? 435  GLU A CD    1 
ATOM   3248 O OE1   . GLU A 1 435 ? -29.087 -1.552  27.790  1.00 30.00 ? 435  GLU A OE1   1 
ATOM   3249 O OE2   . GLU A 1 435 ? -27.532 -0.918  26.374  1.00 30.00 ? 435  GLU A OE2   1 
ATOM   3250 N N     . ALA A 1 436 ? -31.658 -4.572  24.075  1.00 15.06 ? 436  ALA A N     1 
ATOM   3251 C CA    . ALA A 1 436 ? -31.171 -5.660  23.197  1.00 13.73 ? 436  ALA A CA    1 
ATOM   3252 C C     . ALA A 1 436 ? -31.790 -5.533  21.801  1.00 13.33 ? 436  ALA A C     1 
ATOM   3253 O O     . ALA A 1 436 ? -31.064 -5.572  20.819  1.00 13.74 ? 436  ALA A O     1 
ATOM   3254 C CB    . ALA A 1 436 ? -31.495 -6.990  23.813  1.00 15.00 ? 436  ALA A CB    1 
ATOM   3255 N N     . LEU A 1 437 ? -33.112 -5.373  21.762  1.00 13.69 ? 437  LEU A N     1 
ATOM   3256 C CA    . LEU A 1 437 ? -33.820 -5.304  20.456  1.00 14.18 ? 437  LEU A CA    1 
ATOM   3257 C C     . LEU A 1 437 ? -33.307 -4.098  19.657  1.00 15.76 ? 437  LEU A C     1 
ATOM   3258 O O     . LEU A 1 437 ? -33.019 -4.260  18.478  1.00 14.80 ? 437  LEU A O     1 
ATOM   3259 C CB    . LEU A 1 437 ? -35.322 -5.235  20.717  1.00 14.15 ? 437  LEU A CB    1 
ATOM   3260 C CG    . LEU A 1 437 ? -35.975 -6.556  21.135  1.00 15.21 ? 437  LEU A CG    1 
ATOM   3261 C CD1   . LEU A 1 437 ? -37.397 -6.354  21.621  1.00 16.85 ? 437  LEU A CD1   1 
ATOM   3262 C CD2   . LEU A 1 437 ? -35.931 -7.562  20.001  1.00 15.85 ? 437  LEU A CD2   1 
ATOM   3263 N N     . THR A 1 438 ? -33.211 -2.941  20.301  1.00 14.04 ? 438  THR A N     1 
ATOM   3264 C CA    . THR A 1 438 ? -32.682 -1.746  19.665  1.00 15.99 ? 438  THR A CA    1 
ATOM   3265 C C     . THR A 1 438 ? -31.250 -1.967  19.167  1.00 13.59 ? 438  THR A C     1 
ATOM   3266 O O     . THR A 1 438 ? -30.898 -1.613  18.041  1.00 13.40 ? 438  THR A O     1 
ATOM   3267 C CB    . THR A 1 438 ? -32.712 -0.588  20.685  1.00 19.23 ? 438  THR A CB    1 
ATOM   3268 O OG1   . THR A 1 438 ? -34.092 -0.358  20.950  1.00 24.09 ? 438  THR A OG1   1 
ATOM   3269 C CG2   . THR A 1 438 ? -32.157 0.702   20.121  1.00 23.08 ? 438  THR A CG2   1 
ATOM   3270 N N     . GLY A 1 439 ? -30.407 -2.580  19.998  1.00 13.26 ? 439  GLY A N     1 
ATOM   3271 C CA    . GLY A 1 439 ? -29.045 -2.856  19.574  1.00 13.36 ? 439  GLY A CA    1 
ATOM   3272 C C     . GLY A 1 439 ? -29.003 -3.870  18.425  1.00 12.38 ? 439  GLY A C     1 
ATOM   3273 O O     . GLY A 1 439 ? -28.292 -3.690  17.438  1.00 13.11 ? 439  GLY A O     1 
ATOM   3274 N N     . TYR A 1 440 ? -29.720 -4.976  18.580  1.00 13.46 ? 440  TYR A N     1 
ATOM   3275 C CA    . TYR A 1 440 ? -29.637 -6.058  17.616  1.00 12.69 ? 440  TYR A CA    1 
ATOM   3276 C C     . TYR A 1 440 ? -30.153 -5.638  16.239  1.00 12.26 ? 440  TYR A C     1 
ATOM   3277 O O     . TYR A 1 440 ? -29.509 -6.005  15.240  1.00 12.10 ? 440  TYR A O     1 
ATOM   3278 C CB    . TYR A 1 440 ? -30.431 -7.295  18.010  1.00 12.77 ? 440  TYR A CB    1 
ATOM   3279 C CG    . TYR A 1 440 ? -29.959 -8.022  19.245  1.00 12.50 ? 440  TYR A CG    1 
ATOM   3280 C CD1   . TYR A 1 440 ? -28.630 -7.958  19.674  1.00 13.66 ? 440  TYR A CD1   1 
ATOM   3281 C CD2   . TYR A 1 440 ? -30.859 -8.716  20.044  1.00 12.73 ? 440  TYR A CD2   1 
ATOM   3282 C CE1   . TYR A 1 440 ? -28.229 -8.576  20.848  1.00 12.82 ? 440  TYR A CE1   1 
ATOM   3283 C CE2   . TYR A 1 440 ? -30.454 -9.366  21.208  1.00 12.04 ? 440  TYR A CE2   1 
ATOM   3284 C CZ    . TYR A 1 440 ? -29.152 -9.254  21.638  1.00 13.29 ? 440  TYR A CZ    1 
ATOM   3285 O OH    . TYR A 1 440 ? -28.805 -9.873  22.821  1.00 12.33 ? 440  TYR A OH    1 
ATOM   3286 N N     . TYR A 1 441 ? -31.277 -4.893  16.188  1.00 12.94 ? 441  TYR A N     1 
ATOM   3287 C CA    . TYR A 1 441 ? -31.969 -4.692  14.927  1.00 12.89 ? 441  TYR A CA    1 
ATOM   3288 C C     . TYR A 1 441 ? -32.043 -3.231  14.493  1.00 15.07 ? 441  TYR A C     1 
ATOM   3289 O O     . TYR A 1 441 ? -32.425 -2.968  13.350  1.00 14.01 ? 441  TYR A O     1 
ATOM   3290 C CB    . TYR A 1 441 ? -33.375 -5.268  15.041  1.00 12.71 ? 441  TYR A CB    1 
ATOM   3291 C CG    . TYR A 1 441 ? -33.317 -6.764  15.358  1.00 12.88 ? 441  TYR A CG    1 
ATOM   3292 C CD1   . TYR A 1 441 ? -32.767 -7.678  14.463  1.00 14.21 ? 441  TYR A CD1   1 
ATOM   3293 C CD2   . TYR A 1 441 ? -33.818 -7.243  16.549  1.00 13.13 ? 441  TYR A CD2   1 
ATOM   3294 C CE1   . TYR A 1 441 ? -32.698 -9.031  14.774  1.00 14.37 ? 441  TYR A CE1   1 
ATOM   3295 C CE2   . TYR A 1 441 ? -33.748 -8.588  16.869  1.00 13.55 ? 441  TYR A CE2   1 
ATOM   3296 C CZ    . TYR A 1 441 ? -33.202 -9.488  15.981  1.00 12.69 ? 441  TYR A CZ    1 
ATOM   3297 O OH    . TYR A 1 441 ? -33.217 -10.805 16.389  1.00 14.39 ? 441  TYR A OH    1 
ATOM   3298 N N     . GLY A 1 442 ? -31.764 -2.285  15.399  1.00 15.30 ? 442  GLY A N     1 
ATOM   3299 C CA    . GLY A 1 442 ? -31.809 -0.884  15.004  1.00 14.71 ? 442  GLY A CA    1 
ATOM   3300 C C     . GLY A 1 442 ? -33.128 -0.502  14.327  1.00 14.25 ? 442  GLY A C     1 
ATOM   3301 O O     . GLY A 1 442 ? -34.220 -0.849  14.767  1.00 14.08 ? 442  GLY A O     1 
ATOM   3302 N N     . LYS A 1 443 ? -33.034 0.261   13.239  1.00 16.11 ? 443  LYS A N     1 
ATOM   3303 C CA    . LYS A 1 443 ? -34.236 0.786   12.600  1.00 17.07 ? 443  LYS A CA    1 
ATOM   3304 C C     . LYS A 1 443 ? -34.902 -0.263  11.726  1.00 16.61 ? 443  LYS A C     1 
ATOM   3305 O O     . LYS A 1 443 ? -35.882 0.068   11.062  1.00 19.04 ? 443  LYS A O     1 
ATOM   3306 C CB    . LYS A 1 443 ? -33.935 2.023   11.746  1.00 20.09 ? 443  LYS A CB    1 
ATOM   3307 C CG    . LYS A 1 443 ? -33.439 3.219   12.554  1.00 26.39 ? 443  LYS A CG    1 
ATOM   3308 C CD    . LYS A 1 443 ? -33.083 4.378   11.628  1.00 32.35 ? 443  LYS A CD    1 
ATOM   3309 C CE    . LYS A 1 443 ? -32.346 5.490   12.293  1.00 38.22 ? 443  LYS A CE    1 
ATOM   3310 N NZ    . LYS A 1 443 ? -33.201 6.104   13.315  1.00 42.15 ? 443  LYS A NZ    1 
ATOM   3311 N N     . ASN A 1 444 ? -34.372 -1.502  11.694  1.00 14.92 ? 444  ASN A N     1 
ATOM   3312 C CA    . ASN A 1 444 ? -35.102 -2.592  11.052  1.00 15.42 ? 444  ASN A CA    1 
ATOM   3313 C C     . ASN A 1 444 ? -36.188 -3.138  11.991  1.00 15.15 ? 444  ASN A C     1 
ATOM   3314 O O     . ASN A 1 444 ? -36.992 -3.994  11.616  1.00 15.80 ? 444  ASN A O     1 
ATOM   3315 C CB    . ASN A 1 444 ? -34.149 -3.708  10.608  1.00 14.77 ? 444  ASN A CB    1 
ATOM   3316 C CG    . ASN A 1 444 ? -33.438 -3.403  9.310   1.00 16.39 ? 444  ASN A CG    1 
ATOM   3317 O OD1   . ASN A 1 444 ? -33.878 -2.528  8.541   1.00 16.44 ? 444  ASN A OD1   1 
ATOM   3318 N ND2   . ASN A 1 444 ? -32.335 -4.096  9.051   1.00 14.77 ? 444  ASN A ND2   1 
ATOM   3319 N N     . LEU A 1 445 ? -36.185 -2.703  13.253  1.00 14.90 ? 445  LEU A N     1 
ATOM   3320 C CA    . LEU A 1 445 ? -37.055 -3.306  14.251  1.00 15.37 ? 445  LEU A CA    1 
ATOM   3321 C C     . LEU A 1 445 ? -38.525 -3.219  13.830  1.00 15.92 ? 445  LEU A C     1 
ATOM   3322 O O     . LEU A 1 445 ? -39.262 -4.196  13.960  1.00 14.67 ? 445  LEU A O     1 
ATOM   3323 C CB    . LEU A 1 445 ? -36.842 -2.703  15.637  1.00 16.09 ? 445  LEU A CB    1 
ATOM   3324 C CG    . LEU A 1 445 ? -37.648 -3.353  16.773  1.00 18.39 ? 445  LEU A CG    1 
ATOM   3325 C CD1   . LEU A 1 445 ? -37.414 -4.843  16.883  1.00 19.64 ? 445  LEU A CD1   1 
ATOM   3326 C CD2   . LEU A 1 445 ? -37.351 -2.713  18.123  1.00 20.54 ? 445  LEU A CD2   1 
ATOM   3327 N N     . HIS A 1 446 ? -38.959 -2.048  13.346  1.00 17.19 ? 446  HIS A N     1 
ATOM   3328 C CA    . HIS A 1 446 ? -40.380 -1.868  13.074  1.00 19.16 ? 446  HIS A CA    1 
ATOM   3329 C C     . HIS A 1 446 ? -40.864 -2.841  12.000  1.00 17.01 ? 446  HIS A C     1 
ATOM   3330 O O     . HIS A 1 446 ? -41.901 -3.468  12.164  1.00 16.69 ? 446  HIS A O     1 
ATOM   3331 C CB    . HIS A 1 446 ? -40.701 -0.455  12.578  1.00 23.92 ? 446  HIS A CB    1 
ATOM   3332 C CG    . HIS A 1 446 ? -42.183 -0.248  12.396  1.00 32.61 ? 446  HIS A CG    1 
ATOM   3333 N ND1   . HIS A 1 446 ? -42.745 0.301   11.264  1.00 36.49 ? 446  HIS A ND1   1 
ATOM   3334 C CD2   . HIS A 1 446 ? -43.228 -0.540  13.211  1.00 39.25 ? 446  HIS A CD2   1 
ATOM   3335 C CE1   . HIS A 1 446 ? -44.071 0.353   11.398  1.00 39.20 ? 446  HIS A CE1   1 
ATOM   3336 N NE2   . HIS A 1 446 ? -44.394 -0.160  12.567  1.00 36.89 ? 446  HIS A NE2   1 
ATOM   3337 N N     . ARG A 1 447 ? -40.139 -2.938  10.894  1.00 16.24 ? 447  ARG A N     1 
ATOM   3338 C CA    . ARG A 1 447 ? -40.503 -3.821  9.808   1.00 15.13 ? 447  ARG A CA    1 
ATOM   3339 C C     . ARG A 1 447 ? -40.493 -5.272  10.296  1.00 14.93 ? 447  ARG A C     1 
ATOM   3340 O O     . ARG A 1 447 ? -41.381 -6.056  9.962   1.00 15.13 ? 447  ARG A O     1 
ATOM   3341 C CB    . ARG A 1 447 ? -39.627 -3.619  8.565   1.00 16.99 ? 447  ARG A CB    1 
ATOM   3342 C CG    . ARG A 1 447 ? -40.103 -4.443  7.386   1.00 19.24 ? 447  ARG A CG    1 
ATOM   3343 C CD    . ARG A 1 447 ? -39.212 -4.318  6.173   1.00 18.02 ? 447  ARG A CD    1 
ATOM   3344 N NE    . ARG A 1 447 ? -39.668 -5.205  5.103   1.00 18.49 ? 447  ARG A NE    1 
ATOM   3345 C CZ    . ARG A 1 447 ? -38.943 -5.570  4.069   1.00 19.38 ? 447  ARG A CZ    1 
ATOM   3346 N NH1   . ARG A 1 447 ? -37.736 -5.079  3.919   1.00 19.58 ? 447  ARG A NH1   1 
ATOM   3347 N NH2   . ARG A 1 447 ? -39.447 -6.429  3.204   1.00 20.35 ? 447  ARG A NH2   1 
ATOM   3348 N N     . LEU A 1 448 ? -39.492 -5.635  11.103  1.00 13.15 ? 448  LEU A N     1 
ATOM   3349 C CA    . LEU A 1 448 ? -39.479 -6.989  11.647  1.00 13.13 ? 448  LEU A CA    1 
ATOM   3350 C C     . LEU A 1 448 ? -40.700 -7.299  12.517  1.00 12.82 ? 448  LEU A C     1 
ATOM   3351 O O     . LEU A 1 448 ? -41.197 -8.411  12.460  1.00 14.93 ? 448  LEU A O     1 
ATOM   3352 C CB    . LEU A 1 448 ? -38.191 -7.217  12.425  1.00 13.55 ? 448  LEU A CB    1 
ATOM   3353 C CG    . LEU A 1 448 ? -36.968 -7.322  11.531  1.00 13.22 ? 448  LEU A CG    1 
ATOM   3354 C CD1   . LEU A 1 448 ? -35.685 -7.198  12.366  1.00 15.19 ? 448  LEU A CD1   1 
ATOM   3355 C CD2   . LEU A 1 448 ? -36.961 -8.609  10.752  1.00 14.16 ? 448  LEU A CD2   1 
ATOM   3356 N N     . GLN A 1 449 ? -41.151 -6.342  13.327  1.00 14.41 ? 449  GLN A N     1 
ATOM   3357 C CA    . GLN A 1 449 ? -42.352 -6.547  14.118  1.00 15.54 ? 449  GLN A CA    1 
ATOM   3358 C C     . GLN A 1 449 ? -43.580 -6.723  13.219  1.00 16.73 ? 449  GLN A C     1 
ATOM   3359 O O     . GLN A 1 449 ? -44.451 -7.530  13.529  1.00 16.76 ? 449  GLN A O     1 
ATOM   3360 C CB    . GLN A 1 449 ? -42.558 -5.373  15.066  1.00 16.62 ? 449  GLN A CB    1 
ATOM   3361 C CG    . GLN A 1 449 ? -41.540 -5.351  16.198  1.00 17.28 ? 449  GLN A CG    1 
ATOM   3362 C CD    . GLN A 1 449 ? -41.985 -4.430  17.291  1.00 20.96 ? 449  GLN A CD    1 
ATOM   3363 O OE1   . GLN A 1 449 ? -41.633 -3.250  17.275  1.00 23.75 ? 449  GLN A OE1   1 
ATOM   3364 N NE2   . GLN A 1 449 ? -42.814 -4.953  18.185  1.00 21.29 ? 449  GLN A NE2   1 
ATOM   3365 N N     . GLN A 1 450 ? -43.658 -5.957  12.135  1.00 16.74 ? 450  GLN A N     1 
ATOM   3366 C CA    . GLN A 1 450 ? -44.741 -6.120  11.162  1.00 18.41 ? 450  GLN A CA    1 
ATOM   3367 C C     . GLN A 1 450 ? -44.748 -7.530  10.585  1.00 17.06 ? 450  GLN A C     1 
ATOM   3368 O O     . GLN A 1 450 ? -45.784 -8.173  10.510  1.00 17.69 ? 450  GLN A O     1 
ATOM   3369 C CB    . GLN A 1 450 ? -44.602 -5.146  9.992   1.00 19.26 ? 450  GLN A CB    1 
ATOM   3370 C CG    . GLN A 1 450 ? -44.823 -3.696  10.382  1.00 23.20 ? 450  GLN A CG    1 
ATOM   3371 C CD    . GLN A 1 450 ? -44.646 -2.708  9.245   1.00 26.41 ? 450  GLN A CD    1 
ATOM   3372 O OE1   . GLN A 1 450 ? -43.763 -2.835  8.386   1.00 31.84 ? 450  GLN A OE1   1 
ATOM   3373 N NE2   . GLN A 1 450 ? -45.503 -1.699  9.217   1.00 33.17 ? 450  GLN A NE2   1 
ATOM   3374 N N     . ILE A 1 451 ? -43.572 -8.007  10.181  1.00 15.58 ? 451  ILE A N     1 
ATOM   3375 C CA    . ILE A 1 451 ? -43.454 -9.345  9.628   1.00 15.45 ? 451  ILE A CA    1 
ATOM   3376 C C     . ILE A 1 451 ? -43.766 -10.390 10.690  1.00 15.49 ? 451  ILE A C     1 
ATOM   3377 O O     . ILE A 1 451 ? -44.461 -11.364 10.430  1.00 14.97 ? 451  ILE A O     1 
ATOM   3378 C CB    . ILE A 1 451 ? -42.076 -9.537  8.978   1.00 14.79 ? 451  ILE A CB    1 
ATOM   3379 C CG1   . ILE A 1 451 ? -41.884 -8.533  7.817   1.00 16.10 ? 451  ILE A CG1   1 
ATOM   3380 C CG2   . ILE A 1 451 ? -41.861 -10.992 8.550   1.00 15.51 ? 451  ILE A CG2   1 
ATOM   3381 C CD1   . ILE A 1 451 ? -40.469 -8.407  7.298   1.00 15.35 ? 451  ILE A CD1   1 
ATOM   3382 N N     . LYS A 1 452 ? -43.236 -10.190 11.901  1.00 14.91 ? 452  LYS A N     1 
ATOM   3383 C CA    . LYS A 1 452 ? -43.576 -11.064 13.014  1.00 13.89 ? 452  LYS A CA    1 
ATOM   3384 C C     . LYS A 1 452 ? -45.089 -11.185 13.177  1.00 14.55 ? 452  LYS A C     1 
ATOM   3385 O O     . LYS A 1 452 ? -45.592 -12.292 13.331  1.00 14.57 ? 452  LYS A O     1 
ATOM   3386 C CB    . LYS A 1 452 ? -42.906 -10.540 14.284  1.00 14.09 ? 452  LYS A CB    1 
ATOM   3387 C CG    . LYS A 1 452 ? -43.222 -11.345 15.532  1.00 14.54 ? 452  LYS A CG    1 
ATOM   3388 C CD    . LYS A 1 452 ? -42.519 -12.685 15.680  1.00 14.68 ? 452  LYS A CD    1 
ATOM   3389 C CE    . LYS A 1 452 ? -42.954 -13.410 16.930  1.00 15.76 ? 452  LYS A CE    1 
ATOM   3390 N NZ    . LYS A 1 452 ? -42.188 -14.651 17.108  1.00 15.17 ? 452  LYS A NZ    1 
ATOM   3391 N N     . SER A 1 453 ? -45.809 -10.058 13.182  1.00 16.06 ? 453  SER A N     1 
ATOM   3392 C CA    . SER A 1 453 ? -47.267 -10.097 13.329  1.00 16.99 ? 453  SER A CA    1 
ATOM   3393 C C     . SER A 1 453 ? -47.932 -10.878 12.199  1.00 17.82 ? 453  SER A C     1 
ATOM   3394 O O     . SER A 1 453 ? -48.915 -11.575 12.417  1.00 21.32 ? 453  SER A O     1 
ATOM   3395 C CB    . SER A 1 453 ? -47.857 -8.707  13.395  1.00 17.76 ? 453  SER A CB    1 
ATOM   3396 O OG    . SER A 1 453 ? -47.539 -8.154  14.664  1.00 19.27 ? 453  SER A OG    1 
ATOM   3397 N N     . ALA A 1 454 ? -47.418 -10.719 10.989  1.00 18.27 ? 454  ALA A N     1 
ATOM   3398 C CA    . ALA A 1 454 ? -47.922 -11.389 9.808   1.00 18.27 ? 454  ALA A CA    1 
ATOM   3399 C C     . ALA A 1 454 ? -47.724 -12.901 9.890   1.00 20.39 ? 454  ALA A C     1 
ATOM   3400 O O     . ALA A 1 454 ? -48.702 -13.632 9.754   1.00 24.39 ? 454  ALA A O     1 
ATOM   3401 C CB    . ALA A 1 454 ? -47.284 -10.811 8.596   1.00 19.71 ? 454  ALA A CB    1 
ATOM   3402 N N     . VAL A 1 455 ? -46.509 -13.383 10.209  1.00 15.74 ? 455  VAL A N     1 
ATOM   3403 C CA    . VAL A 1 455 ? -46.226 -14.813 10.098  1.00 16.20 ? 455  VAL A CA    1 
ATOM   3404 C C     . VAL A 1 455 ? -46.280 -15.591 11.416  1.00 14.67 ? 455  VAL A C     1 
ATOM   3405 O O     . VAL A 1 455 ? -46.349 -16.827 11.396  1.00 13.44 ? 455  VAL A O     1 
ATOM   3406 C CB    . VAL A 1 455 ? -44.884 -15.033 9.377   1.00 16.78 ? 455  VAL A CB    1 
ATOM   3407 C CG1   . VAL A 1 455 ? -44.872 -14.336 8.028   1.00 19.23 ? 455  VAL A CG1   1 
ATOM   3408 C CG2   . VAL A 1 455 ? -43.691 -14.655 10.232  1.00 17.40 ? 455  VAL A CG2   1 
ATOM   3409 N N     . ASP A 1 456 ? -46.210 -14.898 12.555  1.00 14.68 ? 456  ASP A N     1 
ATOM   3410 C CA    . ASP A 1 456 ? -46.242 -15.567 13.845  1.00 14.17 ? 456  ASP A CA    1 
ATOM   3411 C C     . ASP A 1 456 ? -46.935 -14.652 14.850  1.00 15.77 ? 456  ASP A C     1 
ATOM   3412 O O     . ASP A 1 456 ? -46.333 -14.253 15.847  1.00 15.44 ? 456  ASP A O     1 
ATOM   3413 C CB    . ASP A 1 456 ? -44.817 -15.899 14.283  1.00 13.92 ? 456  ASP A CB    1 
ATOM   3414 C CG    . ASP A 1 456 ? -44.718 -16.726 15.550  1.00 12.00 ? 456  ASP A CG    1 
ATOM   3415 O OD1   . ASP A 1 456 ? -45.733 -17.351 15.939  1.00 13.28 ? 456  ASP A OD1   1 
ATOM   3416 O OD2   . ASP A 1 456 ? -43.628 -16.688 16.182  1.00 13.20 ? 456  ASP A OD2   1 
ATOM   3417 N N     . PRO A 1 457 ? -48.229 -14.307 14.641  1.00 15.25 ? 457  PRO A N     1 
ATOM   3418 C CA    . PRO A 1 457 ? -48.950 -13.414 15.550  1.00 17.41 ? 457  PRO A CA    1 
ATOM   3419 C C     . PRO A 1 457 ? -49.027 -13.916 16.992  1.00 16.51 ? 457  PRO A C     1 
ATOM   3420 O O     . PRO A 1 457 ? -49.088 -13.107 17.889  1.00 17.71 ? 457  PRO A O     1 
ATOM   3421 C CB    . PRO A 1 457 ? -50.374 -13.349 14.892  1.00 17.14 ? 457  PRO A CB    1 
ATOM   3422 C CG    . PRO A 1 457 ? -50.452 -14.678 14.187  1.00 16.26 ? 457  PRO A CG    1 
ATOM   3423 C CD    . PRO A 1 457 ? -49.082 -14.828 13.554  1.00 17.82 ? 457  PRO A CD    1 
ATOM   3424 N N     . ASN A 1 458 ? -49.040 -15.235 17.200  1.00 15.56 ? 458  ASN A N     1 
ATOM   3425 C CA    . ASN A 1 458 ? -49.178 -15.843 18.521  1.00 16.46 ? 458  ASN A CA    1 
ATOM   3426 C C     . ASN A 1 458 ? -47.821 -16.076 19.205  1.00 14.76 ? 458  ASN A C     1 
ATOM   3427 O O     . ASN A 1 458 ? -47.783 -16.590 20.317  1.00 15.53 ? 458  ASN A O     1 
ATOM   3428 C CB    . ASN A 1 458 ? -49.974 -17.141 18.449  1.00 17.03 ? 458  ASN A CB    1 
ATOM   3429 C CG    . ASN A 1 458 ? -51.369 -16.877 17.942  1.00 21.81 ? 458  ASN A CG    1 
ATOM   3430 O OD1   . ASN A 1 458 ? -51.934 -15.814 18.208  1.00 24.61 ? 458  ASN A OD1   1 
ATOM   3431 N ND2   . ASN A 1 458 ? -51.947 -17.820 17.234  1.00 23.01 ? 458  ASN A ND2   1 
ATOM   3432 N N     . ASP A 1 459 ? -46.729 -15.664 18.563  1.00 13.79 ? 459  ASP A N     1 
ATOM   3433 C CA    . ASP A 1 459 ? -45.386 -15.693 19.153  1.00 13.77 ? 459  ASP A CA    1 
ATOM   3434 C C     . ASP A 1 459 ? -45.023 -17.104 19.583  1.00 13.46 ? 459  ASP A C     1 
ATOM   3435 O O     . ASP A 1 459 ? -44.507 -17.316 20.688  1.00 14.63 ? 459  ASP A O     1 
ATOM   3436 C CB    . ASP A 1 459 ? -45.231 -14.703 20.303  1.00 13.62 ? 459  ASP A CB    1 
ATOM   3437 C CG    . ASP A 1 459 ? -43.802 -14.439 20.781  1.00 15.05 ? 459  ASP A CG    1 
ATOM   3438 O OD1   . ASP A 1 459 ? -42.876 -14.471 19.919  1.00 15.07 ? 459  ASP A OD1   1 
ATOM   3439 O OD2   . ASP A 1 459 ? -43.617 -14.137 21.980  1.00 15.84 ? 459  ASP A OD2   1 
ATOM   3440 N N     . VAL A 1 460 ? -45.156 -18.036 18.646  1.00 12.63 ? 460  VAL A N     1 
ATOM   3441 C CA    . VAL A 1 460 ? -44.723 -19.401 18.850  1.00 13.08 ? 460  VAL A CA    1 
ATOM   3442 C C     . VAL A 1 460 ? -43.204 -19.431 18.947  1.00 12.26 ? 460  VAL A C     1 
ATOM   3443 O O     . VAL A 1 460 ? -42.683 -20.149 19.787  1.00 12.61 ? 460  VAL A O     1 
ATOM   3444 C CB    . VAL A 1 460 ? -45.238 -20.306 17.724  1.00 13.86 ? 460  VAL A CB    1 
ATOM   3445 C CG1   . VAL A 1 460 ? -44.731 -21.741 17.817  1.00 13.69 ? 460  VAL A CG1   1 
ATOM   3446 C CG2   . VAL A 1 460 ? -46.748 -20.296 17.683  1.00 14.96 ? 460  VAL A CG2   1 
ATOM   3447 N N     . PHE A 1 461 ? -42.524 -18.704 18.048  1.00 13.14 ? 461  PHE A N     1 
ATOM   3448 C CA    . PHE A 1 461 ? -41.071 -18.714 17.979  1.00 12.18 ? 461  PHE A CA    1 
ATOM   3449 C C     . PHE A 1 461 ? -40.552 -17.607 18.886  1.00 12.92 ? 461  PHE A C     1 
ATOM   3450 O O     . PHE A 1 461 ? -40.489 -16.447 18.493  1.00 13.78 ? 461  PHE A O     1 
ATOM   3451 C CB    . PHE A 1 461 ? -40.593 -18.546 16.533  1.00 12.85 ? 461  PHE A CB    1 
ATOM   3452 C CG    . PHE A 1 461 ? -41.051 -19.699 15.671  1.00 11.79 ? 461  PHE A CG    1 
ATOM   3453 C CD1   . PHE A 1 461 ? -40.655 -21.006 15.949  1.00 11.25 ? 461  PHE A CD1   1 
ATOM   3454 C CD2   . PHE A 1 461 ? -41.890 -19.460 14.581  1.00 12.90 ? 461  PHE A CD2   1 
ATOM   3455 C CE1   . PHE A 1 461 ? -41.084 -22.066 15.168  1.00 12.03 ? 461  PHE A CE1   1 
ATOM   3456 C CE2   . PHE A 1 461 ? -42.260 -20.521 13.780  1.00 12.95 ? 461  PHE A CE2   1 
ATOM   3457 C CZ    . PHE A 1 461 ? -41.900 -21.794 14.075  1.00 11.85 ? 461  PHE A CZ    1 
ATOM   3458 N N     . HIS A 1 462 ? -40.198 -17.996 20.108  1.00 12.23 ? 462  HIS A N     1 
ATOM   3459 C CA    . HIS A 1 462 ? -39.928 -17.059 21.187  1.00 12.61 ? 462  HIS A CA    1 
ATOM   3460 C C     . HIS A 1 462 ? -38.611 -17.396 21.893  1.00 11.92 ? 462  HIS A C     1 
ATOM   3461 O O     . HIS A 1 462 ? -38.321 -18.558 22.197  1.00 12.45 ? 462  HIS A O     1 
ATOM   3462 C CB    . HIS A 1 462 ? -41.087 -17.110 22.191  1.00 13.23 ? 462  HIS A CB    1 
ATOM   3463 C CG    . HIS A 1 462 ? -40.903 -16.212 23.362  1.00 14.24 ? 462  HIS A CG    1 
ATOM   3464 N ND1   . HIS A 1 462 ? -41.308 -14.894 23.271  1.00 16.90 ? 462  HIS A ND1   1 
ATOM   3465 C CD2   . HIS A 1 462 ? -40.250 -16.333 24.551  1.00 15.13 ? 462  HIS A CD2   1 
ATOM   3466 C CE1   . HIS A 1 462 ? -40.935 -14.254 24.395  1.00 17.61 ? 462  HIS A CE1   1 
ATOM   3467 N NE2   . HIS A 1 462 ? -40.309 -15.102 25.176  1.00 16.16 ? 462  HIS A NE2   1 
ATOM   3468 N N     . ASN A 1 463 ? -37.880 -16.343 22.260  1.00 11.65 ? 463  ASN A N     1 
ATOM   3469 C CA    . ASN A 1 463 ? -36.797 -16.459 23.222  1.00 11.40 ? 463  ASN A CA    1 
ATOM   3470 C C     . ASN A 1 463 ? -36.812 -15.167 24.035  1.00 11.89 ? 463  ASN A C     1 
ATOM   3471 O O     . ASN A 1 463 ? -37.634 -14.273 23.799  1.00 12.48 ? 463  ASN A O     1 
ATOM   3472 C CB    . ASN A 1 463 ? -35.432 -16.758 22.578  1.00 11.78 ? 463  ASN A CB    1 
ATOM   3473 C CG    . ASN A 1 463 ? -34.998 -15.713 21.576  1.00 12.15 ? 463  ASN A CG    1 
ATOM   3474 O OD1   . ASN A 1 463 ? -34.778 -14.553 21.958  1.00 12.24 ? 463  ASN A OD1   1 
ATOM   3475 N ND2   . ASN A 1 463 ? -34.869 -16.104 20.295  1.00 12.68 ? 463  ASN A ND2   1 
ATOM   3476 N N     . GLN A 1 464 ? -35.876 -15.077 24.989  1.00 12.07 ? 464  GLN A N     1 
ATOM   3477 C CA    . GLN A 1 464 ? -35.818 -13.952 25.906  1.00 13.04 ? 464  GLN A CA    1 
ATOM   3478 C C     . GLN A 1 464 ? -35.829 -12.625 25.154  1.00 13.80 ? 464  GLN A C     1 
ATOM   3479 O O     . GLN A 1 464 ? -36.353 -11.624 25.653  1.00 16.11 ? 464  GLN A O     1 
ATOM   3480 C CB    . GLN A 1 464 ? -34.575 -14.089 26.782  1.00 12.42 ? 464  GLN A CB    1 
ATOM   3481 C CG    . GLN A 1 464 ? -34.478 -12.964 27.803  1.00 13.15 ? 464  GLN A CG    1 
ATOM   3482 C CD    . GLN A 1 464 ? -33.204 -13.059 28.602  1.00 14.58 ? 464  GLN A CD    1 
ATOM   3483 O OE1   . GLN A 1 464 ? -32.815 -14.136 29.049  1.00 15.98 ? 464  GLN A OE1   1 
ATOM   3484 N NE2   . GLN A 1 464 ? -32.549 -11.924 28.767  1.00 15.32 ? 464  GLN A NE2   1 
ATOM   3485 N N     . GLN A 1 465 ? -35.185 -12.578 23.991  1.00 11.74 ? 465  GLN A N     1 
ATOM   3486 C CA    . GLN A 1 465 ? -34.971 -11.327 23.279  1.00 12.64 ? 465  GLN A CA    1 
ATOM   3487 C C     . GLN A 1 465 ? -35.473 -11.401 21.836  1.00 13.63 ? 465  GLN A C     1 
ATOM   3488 O O     . GLN A 1 465 ? -34.978 -10.696 20.965  1.00 12.97 ? 465  GLN A O     1 
ATOM   3489 C CB    . GLN A 1 465 ? -33.482 -10.983 23.347  1.00 12.67 ? 465  GLN A CB    1 
ATOM   3490 C CG    . GLN A 1 465 ? -33.005 -10.745 24.775  1.00 13.60 ? 465  GLN A CG    1 
ATOM   3491 C CD    . GLN A 1 465 ? -31.526 -10.510 24.869  1.00 12.95 ? 465  GLN A CD    1 
ATOM   3492 O OE1   . GLN A 1 465 ? -30.766 -11.087 24.102  1.00 12.85 ? 465  GLN A OE1   1 
ATOM   3493 N NE2   . GLN A 1 465 ? -31.100 -9.719  25.846  1.00 13.25 ? 465  GLN A NE2   1 
ATOM   3494 N N     . SER A 1 466 ? -36.544 -12.178 21.594  1.00 14.65 ? 466  SER A N     1 
ATOM   3495 C CA    . SER A 1 466 ? -37.116 -12.302 20.264  1.00 13.96 ? 466  SER A CA    1 
ATOM   3496 C C     . SER A 1 466 ? -37.974 -11.079 19.940  1.00 15.03 ? 466  SER A C     1 
ATOM   3497 O O     . SER A 1 466 ? -38.359 -10.273 20.794  1.00 14.36 ? 466  SER A O     1 
ATOM   3498 C CB    . SER A 1 466 ? -37.835 -13.611 20.086  1.00 13.01 ? 466  SER A CB    1 
ATOM   3499 O OG    . SER A 1 466 ? -38.815 -13.813 21.093  1.00 13.43 ? 466  SER A OG    1 
ATOM   3500 N N     . ILE A 1 467 ? -38.220 -10.926 18.651  1.00 16.47 ? 467  ILE A N     1 
ATOM   3501 C CA    . ILE A 1 467 ? -38.945 -9.784  18.123  1.00 16.45 ? 467  ILE A CA    1 
ATOM   3502 C C     . ILE A 1 467 ? -40.404 -9.966  18.499  1.00 15.97 ? 467  ILE A C     1 
ATOM   3503 O O     . ILE A 1 467 ? -41.017 -10.994 18.183  1.00 15.04 ? 467  ILE A O     1 
ATOM   3504 C CB    . ILE A 1 467 ? -38.764 -9.671  16.603  1.00 17.43 ? 467  ILE A CB    1 
ATOM   3505 C CG1   . ILE A 1 467 ? -37.314 -9.277  16.255  1.00 18.92 ? 467  ILE A CG1   1 
ATOM   3506 C CG2   . ILE A 1 467 ? -39.764 -8.667  16.001  1.00 16.85 ? 467  ILE A CG2   1 
ATOM   3507 C CD1   . ILE A 1 467 ? -36.884 -9.796  14.915  1.00 20.84 ? 467  ILE A CD1   1 
ATOM   3508 N N     . PRO A 1 468 ? -40.968 -9.018  19.240  1.00 15.75 ? 468  PRO A N     1 
ATOM   3509 C CA    . PRO A 1 468 ? -42.368 -9.128  19.619  1.00 16.94 ? 468  PRO A CA    1 
ATOM   3510 C C     . PRO A 1 468 ? -43.323 -8.747  18.496  1.00 15.91 ? 468  PRO A C     1 
ATOM   3511 O O     . PRO A 1 468 ? -43.045 -7.855  17.711  1.00 16.67 ? 468  PRO A O     1 
ATOM   3512 C CB    . PRO A 1 468 ? -42.501 -8.177  20.802  1.00 18.10 ? 468  PRO A CB    1 
ATOM   3513 C CG    . PRO A 1 468 ? -41.324 -7.262  20.748  1.00 18.90 ? 468  PRO A CG    1 
ATOM   3514 C CD    . PRO A 1 468 ? -40.311 -7.826  19.783  1.00 17.89 ? 468  PRO A CD    1 
ATOM   3515 N N     . PRO A 1 469 ? -44.501 -9.406  18.412  1.00 18.16 ? 469  PRO A N     1 
ATOM   3516 C CA    . PRO A 1 469 ? -45.533 -8.953  17.486  1.00 19.15 ? 469  PRO A CA    1 
ATOM   3517 C C     . PRO A 1 469 ? -45.870 -7.505  17.852  1.00 21.77 ? 469  PRO A C     1 
ATOM   3518 O O     . PRO A 1 469 ? -45.699 -7.099  19.002  1.00 22.32 ? 469  PRO A O     1 
ATOM   3519 C CB    . PRO A 1 469 ? -46.715 -9.909  17.747  1.00 18.25 ? 469  PRO A CB    1 
ATOM   3520 C CG    . PRO A 1 469 ? -46.153 -11.059 18.511  1.00 20.32 ? 469  PRO A CG    1 
ATOM   3521 C CD    . PRO A 1 469 ? -44.878 -10.595 19.188  1.00 18.63 ? 469  PRO A CD    1 
ATOM   3522 N N     . LEU A 1 470 ? -46.365 -6.744  16.888  1.00 22.59 ? 470  LEU A N     1 
ATOM   3523 C CA    . LEU A 1 470 ? -46.951 -5.426  17.160  1.00 28.44 ? 470  LEU A CA    1 
ATOM   3524 C C     . LEU A 1 470 ? -47.946 -5.469  18.344  1.00 25.68 ? 470  LEU A C     1 
ATOM   3525 O O     . LEU A 1 470 ? -48.743 -6.459  18.504  1.00 28.04 ? 470  LEU A O     1 
ATOM   3526 C CB    . LEU A 1 470 ? -47.643 -4.934  15.894  1.00 26.92 ? 470  LEU A CB    1 
ATOM   3527 C CG    . LEU A 1 470 ? -46.753 -4.688  14.670  1.00 28.17 ? 470  LEU A CG    1 
ATOM   3528 C CD1   . LEU A 1 470 ? -47.632 -4.611  13.443  1.00 31.82 ? 470  LEU A CD1   1 
ATOM   3529 C CD2   . LEU A 1 470 ? -45.956 -3.419  14.813  1.00 30.55 ? 470  LEU A CD2   1 
HETATM 3530 C C1    . NAG B 2 .   ? -8.079  -9.693  34.888  1.00 15.27 ? 1    NAG B C1    1 
HETATM 3531 C C2    . NAG B 2 .   ? -7.620  -10.103 36.297  1.00 16.40 ? 1    NAG B C2    1 
HETATM 3532 C C3    . NAG B 2 .   ? -6.535  -11.176 36.272  1.00 15.83 ? 1    NAG B C3    1 
HETATM 3533 C C4    . NAG B 2 .   ? -6.840  -12.262 35.252  1.00 18.12 ? 1    NAG B C4    1 
HETATM 3534 C C5    . NAG B 2 .   ? -7.022  -11.598 33.894  1.00 15.65 ? 1    NAG B C5    1 
HETATM 3535 C C6    . NAG B 2 .   ? -7.243  -12.561 32.753  1.00 15.49 ? 1    NAG B C6    1 
HETATM 3536 C C7    . NAG B 2 .   ? -7.954  -8.363  37.979  1.00 17.71 ? 1    NAG B C7    1 
HETATM 3537 C C8    . NAG B 2 .   ? -7.420  -7.081  38.539  1.00 19.33 ? 1    NAG B C8    1 
HETATM 3538 N N2    . NAG B 2 .   ? -7.193  -8.952  37.061  1.00 16.70 ? 1    NAG B N2    1 
HETATM 3539 O O3    . NAG B 2 .   ? -6.438  -11.729 37.575  1.00 17.06 ? 1    NAG B O3    1 
HETATM 3540 O O4    . NAG B 2 .   ? -5.754  -13.182 35.229  1.00 18.84 ? 1    NAG B O4    1 
HETATM 3541 O O5    . NAG B 2 .   ? -8.200  -10.784 33.987  1.00 14.53 ? 1    NAG B O5    1 
HETATM 3542 O O6    . NAG B 2 .   ? -8.175  -13.559 33.105  1.00 15.41 ? 1    NAG B O6    1 
HETATM 3543 O O7    . NAG B 2 .   ? -9.023  -8.836  38.344  1.00 16.81 ? 1    NAG B O7    1 
HETATM 3544 C C1    . NAG B 2 .   ? -5.949  -14.555 35.347  1.00 25.78 ? 2    NAG B C1    1 
HETATM 3545 C C2    . NAG B 2 .   ? -4.763  -15.285 34.720  1.00 27.84 ? 2    NAG B C2    1 
HETATM 3546 C C3    . NAG B 2 .   ? -4.980  -16.788 34.836  1.00 31.01 ? 2    NAG B C3    1 
HETATM 3547 C C4    . NAG B 2 .   ? -5.262  -17.183 36.281  1.00 31.87 ? 2    NAG B C4    1 
HETATM 3548 C C5    . NAG B 2 .   ? -6.383  -16.319 36.854  1.00 30.81 ? 2    NAG B C5    1 
HETATM 3549 C C6    . NAG B 2 .   ? -6.602  -16.535 38.328  1.00 31.20 ? 2    NAG B C6    1 
HETATM 3550 C C7    . NAG B 2 .   ? -3.454  -14.162 32.977  1.00 30.64 ? 2    NAG B C7    1 
HETATM 3551 C C8    . NAG B 2 .   ? -2.941  -14.394 31.591  1.00 25.21 ? 2    NAG B C8    1 
HETATM 3552 N N2    . NAG B 2 .   ? -4.504  -14.896 33.347  1.00 32.64 ? 2    NAG B N2    1 
HETATM 3553 O O3    . NAG B 2 .   ? -3.808  -17.405 34.328  1.00 31.86 ? 2    NAG B O3    1 
HETATM 3554 O O4    . NAG B 2 .   ? -5.702  -18.535 36.369  1.00 39.96 ? 2    NAG B O4    1 
HETATM 3555 O O5    . NAG B 2 .   ? -6.064  -14.924 36.706  1.00 23.37 ? 2    NAG B O5    1 
HETATM 3556 O O6    . NAG B 2 .   ? -5.525  -15.991 39.077  1.00 38.13 ? 2    NAG B O6    1 
HETATM 3557 O O7    . NAG B 2 .   ? -2.932  -13.338 33.722  1.00 27.50 ? 2    NAG B O7    1 
HETATM 3558 C C1    . MAN B 2 .   ? -5.023  -19.613 35.807  1.00 39.73 ? 3    MAN B C1    1 
HETATM 3559 C C2    . MAN B 2 .   ? -5.746  -20.844 36.256  1.00 44.98 ? 3    MAN B C2    1 
HETATM 3560 C C3    . MAN B 2 .   ? -4.802  -21.899 36.767  1.00 47.34 ? 3    MAN B C3    1 
HETATM 3561 C C4    . MAN B 2 .   ? -3.661  -22.023 35.793  1.00 46.81 ? 3    MAN B C4    1 
HETATM 3562 C C5    . MAN B 2 .   ? -2.816  -20.768 35.879  1.00 43.71 ? 3    MAN B C5    1 
HETATM 3563 C C6    . MAN B 2 .   ? -1.890  -20.550 34.694  1.00 41.67 ? 3    MAN B C6    1 
HETATM 3564 O O2    . MAN B 2 .   ? -6.499  -21.323 35.149  1.00 39.02 ? 3    MAN B O2    1 
HETATM 3565 O O3    . MAN B 2 .   ? -5.485  -23.144 36.910  1.00 49.21 ? 3    MAN B O3    1 
HETATM 3566 O O4    . MAN B 2 .   ? -2.838  -23.127 36.137  1.00 48.95 ? 3    MAN B O4    1 
HETATM 3567 O O5    . MAN B 2 .   ? -3.619  -19.563 36.071  1.00 42.80 ? 3    MAN B O5    1 
HETATM 3568 O O6    . MAN B 2 .   ? -2.458  -20.407 33.373  1.00 57.13 ? 3    MAN B O6    1 
HETATM 3569 C C1    . MAN B 2 .   ? -2.713  -21.549 32.589  1.00 60.57 ? 4    MAN B C1    1 
HETATM 3570 C C2    . MAN B 2 .   ? -1.476  -21.995 31.816  1.00 64.14 ? 4    MAN B C2    1 
HETATM 3571 C C3    . MAN B 2 .   ? -1.724  -23.393 31.291  1.00 64.36 ? 4    MAN B C3    1 
HETATM 3572 C C4    . MAN B 2 .   ? -3.223  -23.597 31.234  1.00 60.44 ? 4    MAN B C4    1 
HETATM 3573 C C5    . MAN B 2 .   ? -3.843  -22.334 30.641  1.00 59.67 ? 4    MAN B C5    1 
HETATM 3574 C C6    . MAN B 2 .   ? -5.298  -22.488 30.268  1.00 63.73 ? 4    MAN B C6    1 
HETATM 3575 O O2    . MAN B 2 .   ? -0.293  -21.935 32.600  1.00 71.34 ? 4    MAN B O2    1 
HETATM 3576 O O3    . MAN B 2 .   ? -1.124  -24.366 32.141  1.00 56.95 ? 4    MAN B O3    1 
HETATM 3577 O O4    . MAN B 2 .   ? -3.557  -24.749 30.470  1.00 55.23 ? 4    MAN B O4    1 
HETATM 3578 O O5    . MAN B 2 .   ? -3.764  -21.306 31.646  1.00 65.19 ? 4    MAN B O5    1 
HETATM 3579 O O6    . MAN B 2 .   ? -5.868  -21.240 29.874  1.00 63.47 ? 4    MAN B O6    1 
HETATM 3580 C C1    . NAG C 3 .   ? -49.911 -20.092 7.809   1.00 16.02 ? 1    NAG C C1    1 
HETATM 3581 C C2    . NAG C 3 .   ? -51.062 -20.005 6.809   1.00 16.21 ? 1    NAG C C2    1 
HETATM 3582 C C3    . NAG C 3 .   ? -50.603 -19.305 5.536   1.00 16.82 ? 1    NAG C C3    1 
HETATM 3583 C C4    . NAG C 3 .   ? -49.897 -17.993 5.849   1.00 17.06 ? 1    NAG C C4    1 
HETATM 3584 C C5    . NAG C 3 .   ? -48.755 -18.258 6.823   1.00 17.41 ? 1    NAG C C5    1 
HETATM 3585 C C6    . NAG C 3 .   ? -48.025 -17.004 7.239   1.00 18.39 ? 1    NAG C C6    1 
HETATM 3586 C C7    . NAG C 3 .   ? -52.783 -21.704 6.872   1.00 22.82 ? 1    NAG C C7    1 
HETATM 3587 C C8    . NAG C 3 .   ? -53.239 -23.041 6.378   1.00 22.38 ? 1    NAG C C8    1 
HETATM 3588 N N2    . NAG C 3 .   ? -51.574 -21.315 6.483   1.00 18.96 ? 1    NAG C N2    1 
HETATM 3589 O O3    . NAG C 3 .   ? -51.732 -19.094 4.703   1.00 17.93 ? 1    NAG C O3    1 
HETATM 3590 O O4    . NAG C 3 .   ? -49.364 -17.466 4.642   1.00 18.63 ? 1    NAG C O4    1 
HETATM 3591 O O5    . NAG C 3 .   ? -49.293 -18.836 8.024   1.00 15.95 ? 1    NAG C O5    1 
HETATM 3592 O O6    . NAG C 3 .   ? -48.927 -16.058 7.779   1.00 19.46 ? 1    NAG C O6    1 
HETATM 3593 O O7    . NAG C 3 .   ? -53.478 -21.008 7.601   1.00 27.79 ? 1    NAG C O7    1 
HETATM 3594 C C1    . NAG C 3 .   ? -49.677 -16.166 4.255   1.00 23.43 ? 2    NAG C C1    1 
HETATM 3595 C C2    . NAG C 3 .   ? -48.654 -15.704 3.215   1.00 24.86 ? 2    NAG C C2    1 
HETATM 3596 C C3    . NAG C 3 .   ? -49.043 -14.347 2.634   1.00 25.45 ? 2    NAG C C3    1 
HETATM 3597 C C4    . NAG C 3 .   ? -50.513 -14.291 2.240   1.00 29.90 ? 2    NAG C C4    1 
HETATM 3598 C C5    . NAG C 3 .   ? -51.379 -14.741 3.410   1.00 30.11 ? 2    NAG C C5    1 
HETATM 3599 C C6    . NAG C 3 .   ? -52.848 -14.767 3.064   1.00 32.51 ? 2    NAG C C6    1 
HETATM 3600 C C7    . NAG C 3 .   ? -46.349 -16.488 3.602   1.00 24.61 ? 2    NAG C C7    1 
HETATM 3601 C C8    . NAG C 3 .   ? -46.733 -17.750 2.902   1.00 19.68 ? 2    NAG C C8    1 
HETATM 3602 N N2    . NAG C 3 .   ? -47.326 -15.601 3.782   1.00 23.53 ? 2    NAG C N2    1 
HETATM 3603 O O3    . NAG C 3 .   ? -48.218 -14.085 1.511   1.00 25.89 ? 2    NAG C O3    1 
HETATM 3604 O O4    . NAG C 3 .   ? -50.862 -12.951 1.904   1.00 33.72 ? 2    NAG C O4    1 
HETATM 3605 O O5    . NAG C 3 .   ? -51.007 -16.083 3.773   1.00 27.52 ? 2    NAG C O5    1 
HETATM 3606 O O6    . NAG C 3 .   ? -53.151 -15.894 2.257   1.00 37.81 ? 2    NAG C O6    1 
HETATM 3607 O O7    . NAG C 3 .   ? -45.207 -16.288 3.999   1.00 29.52 ? 2    NAG C O7    1 
HETATM 3608 C C1    . NAG D 3 .   ? -34.008 -42.577 15.823  1.00 22.02 ? 1    NAG D C1    1 
HETATM 3609 C C2    . NAG D 3 .   ? -33.327 -42.856 14.490  1.00 26.48 ? 1    NAG D C2    1 
HETATM 3610 C C3    . NAG D 3 .   ? -31.821 -42.765 14.697  1.00 28.28 ? 1    NAG D C3    1 
HETATM 3611 C C4    . NAG D 3 .   ? -31.419 -41.411 15.276  1.00 25.68 ? 1    NAG D C4    1 
HETATM 3612 C C5    . NAG D 3 .   ? -32.294 -41.012 16.461  1.00 22.47 ? 1    NAG D C5    1 
HETATM 3613 C C6    . NAG D 3 .   ? -32.194 -39.534 16.754  1.00 21.46 ? 1    NAG D C6    1 
HETATM 3614 C C7    . NAG D 3 .   ? -34.423 -44.245 12.803  1.00 35.87 ? 1    NAG D C7    1 
HETATM 3615 C C8    . NAG D 3 .   ? -34.492 -43.021 11.943  1.00 36.12 ? 1    NAG D C8    1 
HETATM 3616 N N2    . NAG D 3 .   ? -33.741 -44.131 13.942  1.00 31.87 ? 1    NAG D N2    1 
HETATM 3617 O O3    . NAG D 3 .   ? -31.196 -42.981 13.442  1.00 34.64 ? 1    NAG D O3    1 
HETATM 3618 O O4    . NAG D 3 .   ? -30.079 -41.476 15.749  1.00 27.61 ? 1    NAG D O4    1 
HETATM 3619 O O5    . NAG D 3 .   ? -33.684 -41.248 16.182  1.00 18.18 ? 1    NAG D O5    1 
HETATM 3620 O O6    . NAG D 3 .   ? -32.626 -38.787 15.624  1.00 23.71 ? 1    NAG D O6    1 
HETATM 3621 O O7    . NAG D 3 .   ? -34.956 -45.296 12.468  1.00 52.49 ? 1    NAG D O7    1 
HETATM 3622 C C1    . NAG D 3 .   ? -29.168 -40.612 15.149  1.00 46.48 ? 2    NAG D C1    1 
HETATM 3623 C C2    . NAG D 3 .   ? -28.138 -40.123 16.172  1.00 48.42 ? 2    NAG D C2    1 
HETATM 3624 C C3    . NAG D 3 .   ? -26.834 -39.657 15.525  1.00 52.64 ? 2    NAG D C3    1 
HETATM 3625 C C4    . NAG D 3 .   ? -26.484 -40.445 14.273  1.00 51.94 ? 2    NAG D C4    1 
HETATM 3626 C C5    . NAG D 3 .   ? -27.672 -40.435 13.325  1.00 54.44 ? 2    NAG D C5    1 
HETATM 3627 C C6    . NAG D 3 .   ? -27.387 -41.078 11.991  1.00 56.97 ? 2    NAG D C6    1 
HETATM 3628 C C7    . NAG D 3 .   ? -29.031 -39.053 18.212  1.00 46.46 ? 2    NAG D C7    1 
HETATM 3629 C C8    . NAG D 3 .   ? -28.834 -40.361 18.914  1.00 41.84 ? 2    NAG D C8    1 
HETATM 3630 N N2    . NAG D 3 .   ? -28.665 -39.010 16.932  1.00 43.04 ? 2    NAG D N2    1 
HETATM 3631 O O3    . NAG D 3 .   ? -25.784 -39.752 16.477  1.00 53.51 ? 2    NAG D O3    1 
HETATM 3632 O O4    . NAG D 3 .   ? -25.392 -39.797 13.635  1.00 57.85 ? 2    NAG D O4    1 
HETATM 3633 O O5    . NAG D 3 .   ? -28.714 -41.204 13.947  1.00 45.43 ? 2    NAG D O5    1 
HETATM 3634 O O6    . NAG D 3 .   ? -28.454 -40.835 11.076  1.00 64.82 ? 2    NAG D O6    1 
HETATM 3635 O O7    . NAG D 3 .   ? -29.512 -38.077 18.776  1.00 45.63 ? 2    NAG D O7    1 
HETATM 3636 P PA    . FAD E 4 .   ? -27.977 -22.075 17.972  1.00 11.95 ? 501  FAD A PA    1 
HETATM 3637 O O1A   . FAD E 4 .   ? -28.376 -23.433 17.530  1.00 11.73 ? 501  FAD A O1A   1 
HETATM 3638 O O2A   . FAD E 4 .   ? -27.801 -21.761 19.415  1.00 10.89 ? 501  FAD A O2A   1 
HETATM 3639 O O5B   . FAD E 4 .   ? -28.951 -21.004 17.292  1.00 11.19 ? 501  FAD A O5B   1 
HETATM 3640 C C5B   . FAD E 4 .   ? -28.802 -19.567 17.546  1.00 11.36 ? 501  FAD A C5B   1 
HETATM 3641 C C4B   . FAD E 4 .   ? -30.163 -18.904 17.455  1.00 10.67 ? 501  FAD A C4B   1 
HETATM 3642 O O4B   . FAD E 4 .   ? -30.717 -19.074 16.119  1.00 10.79 ? 501  FAD A O4B   1 
HETATM 3643 C C3B   . FAD E 4 .   ? -31.222 -19.459 18.402  1.00 10.93 ? 501  FAD A C3B   1 
HETATM 3644 O O3B   . FAD E 4 .   ? -32.161 -18.463 18.737  1.00 11.94 ? 501  FAD A O3B   1 
HETATM 3645 C C2B   . FAD E 4 .   ? -31.890 -20.552 17.548  1.00 10.57 ? 501  FAD A C2B   1 
HETATM 3646 O O2B   . FAD E 4 .   ? -33.200 -20.839 18.012  1.00 11.01 ? 501  FAD A O2B   1 
HETATM 3647 C C1B   . FAD E 4 .   ? -31.837 -19.940 16.155  1.00 11.10 ? 501  FAD A C1B   1 
HETATM 3648 N N9A   . FAD E 4 .   ? -31.714 -20.958 15.103  1.00 11.37 ? 501  FAD A N9A   1 
HETATM 3649 C C8A   . FAD E 4 .   ? -30.931 -22.075 15.029  1.00 11.74 ? 501  FAD A C8A   1 
HETATM 3650 N N7A   . FAD E 4 .   ? -31.150 -22.818 13.960  1.00 11.68 ? 501  FAD A N7A   1 
HETATM 3651 C C5A   . FAD E 4 .   ? -32.152 -22.117 13.298  1.00 10.93 ? 501  FAD A C5A   1 
HETATM 3652 C C6A   . FAD E 4 .   ? -32.825 -22.381 12.092  1.00 11.51 ? 501  FAD A C6A   1 
HETATM 3653 N N6A   . FAD E 4 .   ? -32.612 -23.470 11.366  1.00 12.22 ? 501  FAD A N6A   1 
HETATM 3654 N N1A   . FAD E 4 .   ? -33.820 -21.541 11.751  1.00 10.95 ? 501  FAD A N1A   1 
HETATM 3655 C C2A   . FAD E 4 .   ? -34.071 -20.478 12.523  1.00 10.49 ? 501  FAD A C2A   1 
HETATM 3656 N N3A   . FAD E 4 .   ? -33.460 -20.091 13.639  1.00 10.64 ? 501  FAD A N3A   1 
HETATM 3657 C C4A   . FAD E 4 .   ? -32.519 -20.982 13.996  1.00 11.28 ? 501  FAD A C4A   1 
HETATM 3658 N N1    . FAD E 4 .   ? -20.543 -15.290 14.427  1.00 12.18 ? 501  FAD A N1    1 
HETATM 3659 C C2    . FAD E 4 .   ? -19.956 -14.674 13.342  1.00 14.12 ? 501  FAD A C2    1 
HETATM 3660 O O2    . FAD E 4 .   ? -20.599 -14.085 12.471  1.00 12.04 ? 501  FAD A O2    1 
HETATM 3661 N N3    . FAD E 4 .   ? -18.582 -14.746 13.198  1.00 15.95 ? 501  FAD A N3    1 
HETATM 3662 C C4    . FAD E 4 .   ? -17.688 -15.356 14.067  1.00 19.40 ? 501  FAD A C4    1 
HETATM 3663 O O4    . FAD E 4 .   ? -16.505 -15.469 13.777  1.00 22.19 ? 501  FAD A O4    1 
HETATM 3664 C C4X   . FAD E 4 .   ? -18.310 -15.998 15.174  1.00 17.78 ? 501  FAD A C4X   1 
HETATM 3665 N N5    . FAD E 4 .   ? -17.539 -16.638 16.033  1.00 19.87 ? 501  FAD A N5    1 
HETATM 3666 C C5X   . FAD E 4 .   ? -18.161 -17.365 17.024  1.00 14.95 ? 501  FAD A C5X   1 
HETATM 3667 C C6    . FAD E 4 .   ? -17.370 -18.133 17.903  1.00 15.06 ? 501  FAD A C6    1 
HETATM 3668 C C7    . FAD E 4 .   ? -17.935 -18.947 18.858  1.00 14.29 ? 501  FAD A C7    1 
HETATM 3669 C C7M   . FAD E 4 .   ? -17.027 -19.740 19.772  1.00 13.90 ? 501  FAD A C7M   1 
HETATM 3670 C C8    . FAD E 4 .   ? -19.361 -19.052 18.937  1.00 12.51 ? 501  FAD A C8    1 
HETATM 3671 C C8M   . FAD E 4 .   ? -20.056 -19.930 19.955  1.00 13.20 ? 501  FAD A C8M   1 
HETATM 3672 C C9    . FAD E 4 .   ? -20.128 -18.197 18.171  1.00 13.59 ? 501  FAD A C9    1 
HETATM 3673 C C9A   . FAD E 4 .   ? -19.558 -17.395 17.168  1.00 14.16 ? 501  FAD A C9A   1 
HETATM 3674 N N10   . FAD E 4 .   ? -20.316 -16.586 16.332  1.00 13.12 ? 501  FAD A N10   1 
HETATM 3675 C C10   . FAD E 4 .   ? -19.749 -15.923 15.270  1.00 13.78 ? 501  FAD A C10   1 
HETATM 3676 C "C1'" . FAD E 4 .   ? -21.773 -16.453 16.545  1.00 13.30 ? 501  FAD A "C1'" 1 
HETATM 3677 C "C2'" . FAD E 4 .   ? -22.705 -17.339 15.772  1.00 12.91 ? 501  FAD A "C2'" 1 
HETATM 3678 O "O2'" . FAD E 4 .   ? -22.800 -16.751 14.476  1.00 11.77 ? 501  FAD A "O2'" 1 
HETATM 3679 C "C3'" . FAD E 4 .   ? -24.051 -17.324 16.486  1.00 12.53 ? 501  FAD A "C3'" 1 
HETATM 3680 O "O3'" . FAD E 4 .   ? -23.998 -17.707 17.857  1.00 12.32 ? 501  FAD A "O3'" 1 
HETATM 3681 C "C4'" . FAD E 4 .   ? -24.997 -18.236 15.716  1.00 11.47 ? 501  FAD A "C4'" 1 
HETATM 3682 O "O4'" . FAD E 4 .   ? -26.346 -17.840 15.939  1.00 11.00 ? 501  FAD A "O4'" 1 
HETATM 3683 C "C5'" . FAD E 4 .   ? -24.784 -19.656 16.159  1.00 10.07 ? 501  FAD A "C5'" 1 
HETATM 3684 O "O5'" . FAD E 4 .   ? -25.594 -20.523 15.374  1.00 10.11 ? 501  FAD A "O5'" 1 
HETATM 3685 P P     . FAD E 4 .   ? -25.805 -22.010 15.931  1.00 11.16 ? 501  FAD A P     1 
HETATM 3686 O O1P   . FAD E 4 .   ? -26.701 -22.697 14.969  1.00 11.16 ? 501  FAD A O1P   1 
HETATM 3687 O O2P   . FAD E 4 .   ? -24.507 -22.624 16.345  1.00 10.20 ? 501  FAD A O2P   1 
HETATM 3688 O O3P   . FAD E 4 .   ? -26.584 -21.682 17.317  1.00 10.78 ? 501  FAD A O3P   1 
HETATM 3689 C C1    . NAG F 5 .   ? -26.160 -41.548 30.050  1.00 38.40 ? 502  NAG A C1    1 
HETATM 3690 C C2    . NAG F 5 .   ? -26.513 -42.937 29.522  1.00 41.00 ? 502  NAG A C2    1 
HETATM 3691 C C3    . NAG F 5 .   ? -25.445 -43.950 29.922  1.00 45.38 ? 502  NAG A C3    1 
HETATM 3692 C C4    . NAG F 5 .   ? -24.047 -43.409 29.654  1.00 45.31 ? 502  NAG A C4    1 
HETATM 3693 C C5    . NAG F 5 .   ? -23.872 -42.083 30.383  1.00 42.81 ? 502  NAG A C5    1 
HETATM 3694 C C6    . NAG F 5 .   ? -22.503 -41.472 30.204  1.00 43.20 ? 502  NAG A C6    1 
HETATM 3695 C C7    . NAG F 5 .   ? -28.850 -43.558 29.211  1.00 41.76 ? 502  NAG A C7    1 
HETATM 3696 C C8    . NAG F 5 .   ? -30.113 -44.008 29.877  1.00 39.52 ? 502  NAG A C8    1 
HETATM 3697 N N2    . NAG F 5 .   ? -27.806 -43.360 30.012  1.00 38.67 ? 502  NAG A N2    1 
HETATM 3698 O O3    . NAG F 5 .   ? -25.668 -45.161 29.215  1.00 45.74 ? 502  NAG A O3    1 
HETATM 3699 O O4    . NAG F 5 .   ? -23.074 -44.331 30.131  1.00 54.77 ? 502  NAG A O4    1 
HETATM 3700 O O5    . NAG F 5 .   ? -24.818 -41.148 29.837  1.00 35.67 ? 502  NAG A O5    1 
HETATM 3701 O O6    . NAG F 5 .   ? -22.373 -40.870 28.923  1.00 42.41 ? 502  NAG A O6    1 
HETATM 3702 O O7    . NAG F 5 .   ? -28.782 -43.380 28.001  1.00 44.20 ? 502  NAG A O7    1 
HETATM 3703 C C1    . NAG G 5 .   ? 8.842   -1.780  7.327   1.00 55.39 ? 503  NAG A C1    1 
HETATM 3704 C C2    . NAG G 5 .   ? 10.171  -2.095  6.629   1.00 59.87 ? 503  NAG A C2    1 
HETATM 3705 C C3    . NAG G 5 .   ? 11.325  -1.931  7.612   1.00 63.57 ? 503  NAG A C3    1 
HETATM 3706 C C4    . NAG G 5 .   ? 11.284  -0.572  8.302   1.00 65.76 ? 503  NAG A C4    1 
HETATM 3707 C C5    . NAG G 5 .   ? 9.927   -0.369  8.970   1.00 63.95 ? 503  NAG A C5    1 
HETATM 3708 C C6    . NAG G 5 .   ? 9.769   1.032   9.523   1.00 65.38 ? 503  NAG A C6    1 
HETATM 3709 C C7    . NAG G 5 .   ? 10.036  -3.804  4.796   1.00 58.49 ? 503  NAG A C7    1 
HETATM 3710 C C8    . NAG G 5 .   ? 9.452   -2.818  3.824   1.00 53.74 ? 503  NAG A C8    1 
HETATM 3711 N N2    . NAG G 5 .   ? 10.162  -3.437  6.077   1.00 56.47 ? 503  NAG A N2    1 
HETATM 3712 O O3    . NAG G 5 .   ? 12.526  -2.094  6.876   1.00 61.74 ? 503  NAG A O3    1 
HETATM 3713 O O4    . NAG G 5 .   ? 12.308  -0.490  9.293   1.00 64.17 ? 503  NAG A O4    1 
HETATM 3714 O O5    . NAG G 5 .   ? 8.867   -0.532  8.008   1.00 60.36 ? 503  NAG A O5    1 
HETATM 3715 O O6    . NAG G 5 .   ? 8.686   1.103   10.441  1.00 65.91 ? 503  NAG A O6    1 
HETATM 3716 O O7    . NAG G 5 .   ? 10.367  -4.930  4.439   1.00 67.80 ? 503  NAG A O7    1 
HETATM 3717 S S     . SCN H 6 .   ? -30.974 -31.498 5.755   1.00 38.29 ? 504  SCN A S     1 
HETATM 3718 C C     . SCN H 6 .   ? -31.310 -33.069 5.782   1.00 35.83 ? 504  SCN A C     1 
HETATM 3719 N N     . SCN H 6 .   ? -31.320 -34.236 5.681   1.00 36.04 ? 504  SCN A N     1 
HETATM 3720 O O     . HOH I 7 .   ? -27.049 -14.270 -3.292  1.00 42.13 ? 601  HOH A O     1 
HETATM 3721 O O     . HOH I 7 .   ? -24.446 -6.645  37.927  1.00 35.60 ? 602  HOH A O     1 
HETATM 3722 O O     . HOH I 7 .   ? -12.242 -10.178 11.024  1.00 29.71 ? 603  HOH A O     1 
HETATM 3723 O O     . HOH I 7 .   ? -1.803  6.007   18.490  1.00 28.84 ? 604  HOH A O     1 
HETATM 3724 O O     . HOH I 7 .   ? -29.113 -15.996 -5.441  1.00 52.71 ? 605  HOH A O     1 
HETATM 3725 O O     . HOH I 7 .   ? -14.585 -15.099 12.366  1.00 36.99 ? 606  HOH A O     1 
HETATM 3726 O O     . HOH I 7 .   ? 0.620   3.602   31.608  1.00 31.08 ? 607  HOH A O     1 
HETATM 3727 O O     . HOH I 7 .   ? -12.890 -22.443 17.089  1.00 25.67 ? 608  HOH A O     1 
HETATM 3728 O O     . HOH I 7 .   ? -49.481 -8.368  16.179  1.00 32.13 ? 609  HOH A O     1 
HETATM 3729 O O     . HOH I 7 .   ? 14.018  1.238   9.843   1.00 60.66 ? 610  HOH A O     1 
HETATM 3730 O O     . HOH I 7 .   ? -5.017  9.295   13.627  1.00 43.83 ? 611  HOH A O     1 
HETATM 3731 O O     . HOH I 7 .   ? -19.750 11.767  15.126  1.00 33.59 ? 612  HOH A O     1 
HETATM 3732 O O     . HOH I 7 .   ? -15.869 10.061  14.243  1.00 32.59 ? 613  HOH A O     1 
HETATM 3733 O O     . HOH I 7 .   ? -1.274  6.062   24.831  1.00 26.19 ? 614  HOH A O     1 
HETATM 3734 O O     . HOH I 7 .   ? -42.051 -1.343  7.326   1.00 41.70 ? 615  HOH A O     1 
HETATM 3735 O O     . HOH I 7 .   ? 4.908   -5.197  9.259   1.00 32.46 ? 616  HOH A O     1 
HETATM 3736 O O     . HOH I 7 .   ? -1.808  -19.826 10.492  1.00 32.85 ? 617  HOH A O     1 
HETATM 3737 O O     . HOH I 7 .   ? -31.748 -40.530 28.264  1.00 26.78 ? 618  HOH A O     1 
HETATM 3738 O O     . HOH I 7 .   ? -35.066 -14.120 17.982  1.00 16.94 ? 619  HOH A O     1 
HETATM 3739 O O     . HOH I 7 .   ? 5.422   -8.235  8.559   1.00 38.91 ? 620  HOH A O     1 
HETATM 3740 O O     . HOH I 7 .   ? -41.255 -37.269 6.697   1.00 16.13 ? 621  HOH A O     1 
HETATM 3741 O O     . HOH I 7 .   ? -26.222 5.534   23.676  1.00 27.70 ? 622  HOH A O     1 
HETATM 3742 O O     . HOH I 7 .   ? -1.818  -21.449 -4.114  1.00 32.55 ? 623  HOH A O     1 
HETATM 3743 O O     . HOH I 7 .   ? -35.166 -15.214 -7.368  1.00 44.90 ? 624  HOH A O     1 
HETATM 3744 O O     . HOH I 7 .   ? -21.512 -25.264 39.158  1.00 26.09 ? 625  HOH A O     1 
HETATM 3745 O O     . HOH I 7 .   ? -27.740 -20.030 -7.747  1.00 32.91 ? 626  HOH A O     1 
HETATM 3746 O O     . HOH I 7 .   ? -14.225 3.922   10.231  1.00 32.47 ? 627  HOH A O     1 
HETATM 3747 O O     . HOH I 7 .   ? -4.369  -4.593  38.019  1.00 26.05 ? 628  HOH A O     1 
HETATM 3748 O O     . HOH I 7 .   ? -41.033 -12.748 20.362  1.00 17.51 ? 629  HOH A O     1 
HETATM 3749 O O     . HOH I 7 .   ? -15.894 -6.033  38.446  1.00 19.56 ? 630  HOH A O     1 
HETATM 3750 O O     . HOH I 7 .   ? -25.153 5.169   10.981  1.00 24.17 ? 631  HOH A O     1 
HETATM 3751 O O     . HOH I 7 .   ? -12.297 2.128   6.187   1.00 36.12 ? 632  HOH A O     1 
HETATM 3752 O O     . HOH I 7 .   ? -33.065 -30.198 4.794   1.00 36.15 ? 633  HOH A O     1 
HETATM 3753 O O     . HOH I 7 .   ? -47.773 -15.601 23.722  1.00 27.63 ? 634  HOH A O     1 
HETATM 3754 O O     . HOH I 7 .   ? -19.913 -1.701  36.257  1.00 31.80 ? 635  HOH A O     1 
HETATM 3755 O O     . HOH I 7 .   ? 3.160   -6.336  34.016  1.00 34.39 ? 636  HOH A O     1 
HETATM 3756 O O     . HOH I 7 .   ? -38.463 -18.933 -3.397  1.00 32.08 ? 637  HOH A O     1 
HETATM 3757 O O     . HOH I 7 .   ? -32.790 -14.682 -3.656  1.00 21.05 ? 638  HOH A O     1 
HETATM 3758 O O     . HOH I 7 .   ? -46.357 -21.143 26.229  1.00 45.55 ? 639  HOH A O     1 
HETATM 3759 O O     . HOH I 7 .   ? -17.317 -18.978 23.439  1.00 26.97 ? 640  HOH A O     1 
HETATM 3760 O O     . HOH I 7 .   ? -2.674  -5.668  -1.598  1.00 35.01 ? 641  HOH A O     1 
HETATM 3761 O O     . HOH I 7 .   ? -3.485  -6.216  32.124  1.00 22.74 ? 642  HOH A O     1 
HETATM 3762 O O     . HOH I 7 .   ? -35.714 -27.292 -0.055  1.00 25.53 ? 643  HOH A O     1 
HETATM 3763 O O     . HOH I 7 .   ? -13.899 -27.204 22.846  1.00 37.73 ? 644  HOH A O     1 
HETATM 3764 O O     . HOH I 7 .   ? -33.908 -34.501 5.815   1.00 28.01 ? 645  HOH A O     1 
HETATM 3765 O O     . HOH I 7 .   ? -19.284 4.050   9.064   1.00 20.76 ? 646  HOH A O     1 
HETATM 3766 O O     . HOH I 7 .   ? -34.304 -39.978 24.161  1.00 24.07 ? 647  HOH A O     1 
HETATM 3767 O O     . HOH I 7 .   ? -17.039 -2.021  36.468  1.00 29.35 ? 648  HOH A O     1 
HETATM 3768 O O     . HOH I 7 .   ? -14.828 -17.630 15.536  1.00 31.50 ? 649  HOH A O     1 
HETATM 3769 O O     . HOH I 7 .   ? -22.116 -27.532 17.205  1.00 16.80 ? 650  HOH A O     1 
HETATM 3770 O O     . HOH I 7 .   ? -38.302 -22.545 -5.456  1.00 38.29 ? 651  HOH A O     1 
HETATM 3771 O O     . HOH I 7 .   ? -10.802 -13.022 19.219  1.00 27.59 ? 652  HOH A O     1 
HETATM 3772 O O     . HOH I 7 .   ? -24.473 -8.426  22.120  1.00 15.11 ? 653  HOH A O     1 
HETATM 3773 O O     . HOH I 7 .   ? -16.136 -18.251 38.871  1.00 38.36 ? 654  HOH A O     1 
HETATM 3774 O O     . HOH I 7 .   ? -47.921 -20.255 23.469  1.00 28.68 ? 655  HOH A O     1 
HETATM 3775 O O     . HOH I 7 .   ? -32.557 -36.214 34.356  0.50 20.28 ? 656  HOH A O     1 
HETATM 3776 O O     . HOH I 7 .   ? -42.382 -31.647 29.518  1.00 22.21 ? 657  HOH A O     1 
HETATM 3777 O O     . HOH I 7 .   ? -29.092 4.068   13.325  1.00 34.11 ? 658  HOH A O     1 
HETATM 3778 O O     . HOH I 7 .   ? -46.462 -40.815 13.785  1.00 23.49 ? 659  HOH A O     1 
HETATM 3779 O O     . HOH I 7 .   ? -16.940 -14.118 38.133  1.00 17.55 ? 660  HOH A O     1 
HETATM 3780 O O     . HOH I 7 .   ? -11.855 -22.442 32.823  1.00 31.79 ? 661  HOH A O     1 
HETATM 3781 O O     . HOH I 7 .   ? -23.938 -6.449  24.757  1.00 15.43 ? 662  HOH A O     1 
HETATM 3782 O O     . HOH I 7 .   ? -10.801 4.137   33.148  1.00 21.17 ? 663  HOH A O     1 
HETATM 3783 O O     . HOH I 7 .   ? -31.410 -22.267 35.247  1.00 35.61 ? 664  HOH A O     1 
HETATM 3784 O O     . HOH I 7 .   ? -38.931 -10.112 23.370  1.00 34.47 ? 665  HOH A O     1 
HETATM 3785 O O     . HOH I 7 .   ? -4.028  11.368  18.342  1.00 38.80 ? 666  HOH A O     1 
HETATM 3786 O O     . HOH I 7 .   ? -29.011 -6.710  12.740  1.00 27.69 ? 667  HOH A O     1 
HETATM 3787 O O     . HOH I 7 .   ? -11.908 -10.512 3.650   1.00 13.40 ? 668  HOH A O     1 
HETATM 3788 O O     . HOH I 7 .   ? -45.119 -14.019 24.158  1.00 29.08 ? 669  HOH A O     1 
HETATM 3789 O O     . HOH I 7 .   ? -51.940 -22.748 28.812  1.00 40.84 ? 670  HOH A O     1 
HETATM 3790 O O     . HOH I 7 .   ? 5.238   0.493   27.882  1.00 30.99 ? 671  HOH A O     1 
HETATM 3791 O O     . HOH I 7 .   ? -22.310 -7.948  0.780   1.00 21.43 ? 672  HOH A O     1 
HETATM 3792 O O     . HOH I 7 .   ? -8.926  -13.234 38.066  1.00 21.57 ? 673  HOH A O     1 
HETATM 3793 O O     . HOH I 7 .   ? -16.182 -27.305 26.872  1.00 27.81 ? 674  HOH A O     1 
HETATM 3794 O O     . HOH I 7 .   ? -54.945 -27.632 21.322  1.00 44.64 ? 675  HOH A O     1 
HETATM 3795 O O     . HOH I 7 .   ? -37.771 -11.168 27.852  1.00 32.24 ? 676  HOH A O     1 
HETATM 3796 O O     . HOH I 7 .   ? -12.397 -21.376 10.020  1.00 17.67 ? 677  HOH A O     1 
HETATM 3797 O O     . HOH I 7 .   ? -40.313 -33.939 14.938  1.00 35.09 ? 678  HOH A O     1 
HETATM 3798 O O     . HOH I 7 .   ? -52.617 -26.487 15.865  1.00 32.65 ? 679  HOH A O     1 
HETATM 3799 O O     . HOH I 7 .   ? -25.660 -7.153  33.143  1.00 28.35 ? 680  HOH A O     1 
HETATM 3800 O O     . HOH I 7 .   ? -23.978 7.608   11.501  1.00 30.00 ? 681  HOH A O     1 
HETATM 3801 O O     . HOH I 7 .   ? -20.428 -7.569  -3.287  1.00 30.00 ? 682  HOH A O     1 
HETATM 3802 O O     . HOH I 7 .   ? -32.598 -33.435 13.907  1.00 14.79 ? 683  HOH A O     1 
HETATM 3803 O O     . HOH I 7 .   ? -19.390 -26.563 35.472  1.00 25.89 ? 684  HOH A O     1 
HETATM 3804 O O     . HOH I 7 .   ? -4.182  -10.619 22.851  1.00 25.33 ? 685  HOH A O     1 
HETATM 3805 O O     . HOH I 7 .   ? -37.591 -41.189 34.478  1.00 50.29 ? 686  HOH A O     1 
HETATM 3806 O O     . HOH I 7 .   ? -13.498 -20.661 5.701   1.00 19.04 ? 687  HOH A O     1 
HETATM 3807 O O     . HOH I 7 .   ? -50.644 -24.511 8.212   1.00 17.67 ? 688  HOH A O     1 
HETATM 3808 O O     . HOH I 7 .   ? -10.223 11.031  31.206  1.00 40.48 ? 689  HOH A O     1 
HETATM 3809 O O     . HOH I 7 .   ? -32.431 -37.059 8.254   1.00 30.57 ? 690  HOH A O     1 
HETATM 3810 O O     . HOH I 7 .   ? -20.679 5.590   28.176  1.00 20.94 ? 691  HOH A O     1 
HETATM 3811 O O     . HOH I 7 .   ? -40.115 -26.312 0.095   1.00 19.77 ? 692  HOH A O     1 
HETATM 3812 O O     . HOH I 7 .   ? -50.028 -8.530  19.594  1.00 42.22 ? 693  HOH A O     1 
HETATM 3813 O O     . HOH I 7 .   ? -8.837  -21.541 35.452  1.00 30.77 ? 694  HOH A O     1 
HETATM 3814 O O     . HOH I 7 .   ? -13.692 8.026   29.015  1.00 24.67 ? 695  HOH A O     1 
HETATM 3815 O O     . HOH I 7 .   ? 3.624   4.112   27.831  1.00 39.60 ? 696  HOH A O     1 
HETATM 3816 O O     . HOH I 7 .   ? -13.041 0.072   37.399  1.00 28.29 ? 697  HOH A O     1 
HETATM 3817 O O     . HOH I 7 .   ? -4.187  9.235   23.625  1.00 33.66 ? 698  HOH A O     1 
HETATM 3818 O O     . HOH I 7 .   ? -27.549 -33.228 22.611  1.00 19.84 ? 699  HOH A O     1 
HETATM 3819 O O     . HOH I 7 .   ? -48.194 -7.100  10.067  1.00 27.43 ? 700  HOH A O     1 
HETATM 3820 O O     . HOH I 7 .   ? -18.012 -5.190  27.303  1.00 12.85 ? 701  HOH A O     1 
HETATM 3821 O O     . HOH I 7 .   ? -49.465 -31.376 22.020  1.00 19.74 ? 702  HOH A O     1 
HETATM 3822 O O     . HOH I 7 .   ? -33.256 -9.207  27.853  1.00 15.28 ? 703  HOH A O     1 
HETATM 3823 O O     . HOH I 7 .   ? -36.334 -2.110  7.557   1.00 24.36 ? 704  HOH A O     1 
HETATM 3824 O O     . HOH I 7 .   ? -28.762 -5.374  5.443   1.00 14.79 ? 705  HOH A O     1 
HETATM 3825 O O     . HOH I 7 .   ? -22.791 1.073   12.324  1.00 16.05 ? 706  HOH A O     1 
HETATM 3826 O O     . HOH I 7 .   ? -29.022 -36.667 15.574  1.00 35.93 ? 707  HOH A O     1 
HETATM 3827 O O     . HOH I 7 .   ? -6.164  -6.826  32.441  1.00 19.04 ? 708  HOH A O     1 
HETATM 3828 O O     . HOH I 7 .   ? -29.123 -3.239  -0.749  1.00 24.77 ? 709  HOH A O     1 
HETATM 3829 O O     . HOH I 7 .   ? -33.628 -11.719 18.884  1.00 15.45 ? 710  HOH A O     1 
HETATM 3830 O O     . HOH I 7 .   ? -6.826  -12.395 29.143  1.00 17.74 ? 711  HOH A O     1 
HETATM 3831 O O     . HOH I 7 .   ? -45.341 -9.492  5.586   1.00 33.37 ? 712  HOH A O     1 
HETATM 3832 O O     . HOH I 7 .   ? -31.473 -16.593 13.601  1.00 20.67 ? 713  HOH A O     1 
HETATM 3833 O O     . HOH I 7 .   ? -52.188 -22.480 23.692  1.00 38.85 ? 714  HOH A O     1 
HETATM 3834 O O     . HOH I 7 .   ? -18.418 11.324  10.745  1.00 38.06 ? 715  HOH A O     1 
HETATM 3835 O O     . HOH I 7 .   ? -20.877 -13.877 -6.018  1.00 36.86 ? 716  HOH A O     1 
HETATM 3836 O O     . HOH I 7 .   ? -4.535  -19.574 19.639  1.00 31.83 ? 717  HOH A O     1 
HETATM 3837 O O     . HOH I 7 .   ? -20.298 -10.341 -2.616  1.00 29.14 ? 718  HOH A O     1 
HETATM 3838 O O     . HOH I 7 .   ? -17.738 -11.975 -6.119  1.00 29.68 ? 719  HOH A O     1 
HETATM 3839 O O     . HOH I 7 .   ? -5.707  4.100   6.322   1.00 17.96 ? 720  HOH A O     1 
HETATM 3840 O O     . HOH I 7 .   ? -9.391  -6.272  34.561  1.00 17.21 ? 721  HOH A O     1 
HETATM 3841 O O     . HOH I 7 .   ? -25.901 -27.452 21.999  1.00 21.97 ? 722  HOH A O     1 
HETATM 3842 O O     . HOH I 7 .   ? -15.643 9.830   16.982  1.00 30.36 ? 723  HOH A O     1 
HETATM 3843 O O     . HOH I 7 .   ? -1.172  -24.238 10.373  1.00 31.63 ? 724  HOH A O     1 
HETATM 3844 O O     . HOH I 7 .   ? -10.237 -32.959 -0.289  1.00 25.83 ? 725  HOH A O     1 
HETATM 3845 O O     . HOH I 7 .   ? -47.966 -18.893 10.789  1.00 16.67 ? 726  HOH A O     1 
HETATM 3846 O O     . HOH I 7 .   ? -31.726 -12.524 14.949  1.00 15.36 ? 727  HOH A O     1 
HETATM 3847 O O     . HOH I 7 .   ? -42.608 -38.766 9.469   1.00 22.82 ? 728  HOH A O     1 
HETATM 3848 O O     . HOH I 7 .   ? -4.012  -14.272 13.051  1.00 34.85 ? 729  HOH A O     1 
HETATM 3849 O O     . HOH I 7 .   ? -17.247 -0.634  1.762   1.00 37.18 ? 730  HOH A O     1 
HETATM 3850 O O     . HOH I 7 .   ? -22.671 -29.020 26.721  1.00 25.66 ? 731  HOH A O     1 
HETATM 3851 O O     . HOH I 7 .   ? 8.707   -6.819  15.147  1.00 37.17 ? 732  HOH A O     1 
HETATM 3852 O O     . HOH I 7 .   ? -36.457 -29.387 1.742   1.00 25.50 ? 733  HOH A O     1 
HETATM 3853 O O     . HOH I 7 .   ? -44.394 -4.602  6.445   1.00 39.52 ? 734  HOH A O     1 
HETATM 3854 O O     . HOH I 7 .   ? -26.233 -4.856  30.823  1.00 23.76 ? 735  HOH A O     1 
HETATM 3855 O O     . HOH I 7 .   ? -6.466  -19.197 32.501  1.00 26.32 ? 736  HOH A O     1 
HETATM 3856 O O     . HOH I 7 .   ? -7.324  -24.242 -1.693  1.00 22.93 ? 737  HOH A O     1 
HETATM 3857 O O     . HOH I 7 .   ? -23.224 -20.541 37.262  1.00 35.48 ? 738  HOH A O     1 
HETATM 3858 O O     . HOH I 7 .   ? -47.274 -41.274 20.111  1.00 20.10 ? 739  HOH A O     1 
HETATM 3859 O O     . HOH I 7 .   ? 1.183   2.977   17.426  1.00 29.69 ? 740  HOH A O     1 
HETATM 3860 O O     . HOH I 7 .   ? -27.583 -9.670  0.379   1.00 21.19 ? 741  HOH A O     1 
HETATM 3861 O O     . HOH I 7 .   ? -8.438  -17.749 14.076  1.00 30.05 ? 742  HOH A O     1 
HETATM 3862 O O     . HOH I 7 .   ? -50.305 -10.702 17.613  1.00 24.32 ? 743  HOH A O     1 
HETATM 3863 O O     . HOH I 7 .   ? -4.114  -23.051 14.262  1.00 24.34 ? 744  HOH A O     1 
HETATM 3864 O O     . HOH I 7 .   ? -12.938 -24.260 34.526  1.00 36.38 ? 745  HOH A O     1 
HETATM 3865 O O     . HOH I 7 .   ? -29.228 -25.006 -7.591  1.00 46.31 ? 746  HOH A O     1 
HETATM 3866 O O     . HOH I 7 .   ? -30.928 -18.040 29.046  1.00 18.89 ? 747  HOH A O     1 
HETATM 3867 O O     . HOH I 7 .   ? -10.020 -0.512  3.576   1.00 24.91 ? 748  HOH A O     1 
HETATM 3868 O O     . HOH I 7 .   ? -24.483 -38.654 28.820  1.00 40.63 ? 749  HOH A O     1 
HETATM 3869 O O     . HOH I 7 .   ? -22.807 10.199  16.317  1.00 25.21 ? 750  HOH A O     1 
HETATM 3870 O O     . HOH I 7 .   ? -7.746  -12.870 13.063  1.00 34.44 ? 751  HOH A O     1 
HETATM 3871 O O     . HOH I 7 .   ? -15.564 -25.133 19.542  1.00 24.45 ? 752  HOH A O     1 
HETATM 3872 O O     . HOH I 7 .   ? -15.444 -22.185 32.330  1.00 19.04 ? 753  HOH A O     1 
HETATM 3873 O O     . HOH I 7 .   ? -42.550 -45.670 20.285  1.00 16.78 ? 754  HOH A O     1 
HETATM 3874 O O     . HOH I 7 .   ? -26.967 -1.159  22.202  1.00 18.56 ? 755  HOH A O     1 
HETATM 3875 O O     . HOH I 7 .   ? -28.377 -25.717 24.823  1.00 14.06 ? 756  HOH A O     1 
HETATM 3876 O O     . HOH I 7 .   ? -17.953 6.430   20.682  1.00 16.82 ? 757  HOH A O     1 
HETATM 3877 O O     . HOH I 7 .   ? -48.858 -13.026 20.602  1.00 33.38 ? 758  HOH A O     1 
HETATM 3878 O O     . HOH I 7 .   ? -0.279  -5.754  25.666  1.00 17.25 ? 759  HOH A O     1 
HETATM 3879 O O     . HOH I 7 .   ? -23.365 11.048  23.173  1.00 24.28 ? 760  HOH A O     1 
HETATM 3880 O O     . HOH I 7 .   ? -6.179  -30.702 3.494   1.00 33.75 ? 761  HOH A O     1 
HETATM 3881 O O     . HOH I 7 .   ? -21.959 2.985   16.799  1.00 13.87 ? 762  HOH A O     1 
HETATM 3882 O O     . HOH I 7 .   ? -48.339 -25.411 14.194  1.00 16.15 ? 763  HOH A O     1 
HETATM 3883 O O     . HOH I 7 .   ? -14.581 -14.319 -6.894  1.00 34.55 ? 764  HOH A O     1 
HETATM 3884 O O     . HOH I 7 .   ? -3.171  -3.850  31.429  1.00 22.18 ? 765  HOH A O     1 
HETATM 3885 O O     . HOH I 7 .   ? 2.259   1.064   21.935  1.00 22.16 ? 766  HOH A O     1 
HETATM 3886 O O     . HOH I 7 .   ? -3.518  -30.533 2.789   1.00 34.33 ? 767  HOH A O     1 
HETATM 3887 O O     . HOH I 7 .   ? -5.891  -29.030 7.816   1.00 30.44 ? 768  HOH A O     1 
HETATM 3888 O O     . HOH I 7 .   ? -13.744 -17.176 8.102   1.00 15.85 ? 769  HOH A O     1 
HETATM 3889 O O     . HOH I 7 .   ? -30.851 -15.548 30.333  1.00 20.62 ? 770  HOH A O     1 
HETATM 3890 O O     . HOH I 7 .   ? -36.452 -2.853  5.093   1.00 19.20 ? 771  HOH A O     1 
HETATM 3891 O O     . HOH I 7 .   ? -25.179 0.052   13.416  1.00 16.69 ? 772  HOH A O     1 
HETATM 3892 O O     . HOH I 7 .   ? -5.896  -20.420 0.078   1.00 23.12 ? 773  HOH A O     1 
HETATM 3893 O O     . HOH I 7 .   ? -16.959 0.462   7.246   1.00 25.36 ? 774  HOH A O     1 
HETATM 3894 O O     . HOH I 7 .   ? -13.360 -11.469 22.347  1.00 14.70 ? 775  HOH A O     1 
HETATM 3895 O O     . HOH I 7 .   ? -19.503 8.706   7.311   1.00 34.41 ? 776  HOH A O     1 
HETATM 3896 O O     . HOH I 7 .   ? 2.197   -2.951  27.586  1.00 23.90 ? 777  HOH A O     1 
HETATM 3897 O O     . HOH I 7 .   ? -28.926 -22.524 21.802  1.00 10.47 ? 778  HOH A O     1 
HETATM 3898 O O     . HOH I 7 .   ? -17.227 2.074   33.200  1.00 28.80 ? 779  HOH A O     1 
HETATM 3899 O O     . HOH I 7 .   ? -19.492 -11.024 22.476  1.00 24.85 ? 780  HOH A O     1 
HETATM 3900 O O     . HOH I 7 .   ? -22.048 -12.891 42.186  1.00 29.82 ? 781  HOH A O     1 
HETATM 3901 O O     . HOH I 7 .   ? -17.758 -10.576 -3.813  1.00 24.13 ? 782  HOH A O     1 
HETATM 3902 O O     . HOH I 7 .   ? -5.063  -2.682  29.722  1.00 15.34 ? 783  HOH A O     1 
HETATM 3903 O O     . HOH I 7 .   ? -23.444 -13.179 26.444  1.00 15.57 ? 784  HOH A O     1 
HETATM 3904 O O     . HOH I 7 .   ? -22.051 -32.875 -3.566  1.00 27.54 ? 785  HOH A O     1 
HETATM 3905 O O     . HOH I 7 .   ? -18.722 -18.779 41.534  1.00 30.15 ? 786  HOH A O     1 
HETATM 3906 O O     . HOH I 7 .   ? -28.046 -29.060 -5.255  1.00 24.69 ? 787  HOH A O     1 
HETATM 3907 O O     . HOH I 7 .   ? -4.326  4.195   29.053  1.00 22.08 ? 788  HOH A O     1 
HETATM 3908 O O     . HOH I 7 .   ? -24.005 -23.521 36.380  1.00 19.30 ? 789  HOH A O     1 
HETATM 3909 O O     . HOH I 7 .   ? -8.800  -0.000  0.000   0.50 25.34 ? 790  HOH A O     1 
HETATM 3910 O O     . HOH I 7 .   ? -21.306 -16.841 -6.831  1.00 48.98 ? 791  HOH A O     1 
HETATM 3911 O O     . HOH I 7 .   ? -14.253 -21.133 25.949  1.00 18.41 ? 792  HOH A O     1 
HETATM 3912 O O     . HOH I 7 .   ? -15.261 -21.915 9.694   1.00 35.67 ? 793  HOH A O     1 
HETATM 3913 O O     . HOH I 7 .   ? 6.803   -6.543  12.826  1.00 36.09 ? 794  HOH A O     1 
HETATM 3914 O O     . HOH I 7 .   ? -21.604 -17.403 41.259  1.00 27.40 ? 795  HOH A O     1 
HETATM 3915 O O     . HOH I 7 .   ? 8.714   -12.394 15.356  1.00 39.31 ? 796  HOH A O     1 
HETATM 3916 O O     . HOH I 7 .   ? -27.531 -30.281 16.502  1.00 24.90 ? 797  HOH A O     1 
HETATM 3917 O O     . HOH I 7 .   ? 6.528   -0.879  13.969  1.00 30.00 ? 798  HOH A O     1 
HETATM 3918 O O     . HOH I 7 .   ? -15.371 -6.984  -2.923  1.00 39.82 ? 799  HOH A O     1 
HETATM 3919 O O     . HOH I 7 .   ? -34.908 -17.615 26.008  1.00 13.62 ? 800  HOH A O     1 
HETATM 3920 O O     . HOH I 7 .   ? -7.733  -10.728 -2.995  1.00 39.79 ? 801  HOH A O     1 
HETATM 3921 O O     . HOH I 7 .   ? -21.895 -30.943 10.891  1.00 17.21 ? 802  HOH A O     1 
HETATM 3922 O O     . HOH I 7 .   ? -29.182 -15.083 17.777  1.00 13.28 ? 803  HOH A O     1 
HETATM 3923 O O     . HOH I 7 .   ? -16.678 12.311  20.947  1.00 31.80 ? 804  HOH A O     1 
HETATM 3924 O O     . HOH I 7 .   ? -28.070 -26.461 -5.292  1.00 19.33 ? 805  HOH A O     1 
HETATM 3925 O O     . HOH I 7 .   ? -31.953 -38.544 21.999  1.00 34.51 ? 806  HOH A O     1 
HETATM 3926 O O     . HOH I 7 .   ? 7.341   -3.020  12.754  1.00 42.39 ? 807  HOH A O     1 
HETATM 3927 O O     . HOH I 7 .   ? -48.466 -17.586 15.563  1.00 14.19 ? 808  HOH A O     1 
HETATM 3928 O O     . HOH I 7 .   ? -44.075 -18.397 11.584  1.00 14.27 ? 809  HOH A O     1 
HETATM 3929 O O     . HOH I 7 .   ? -34.974 -38.849 14.257  1.00 27.01 ? 810  HOH A O     1 
HETATM 3930 O O     . HOH I 7 .   ? -32.704 -29.714 32.575  1.00 13.47 ? 811  HOH A O     1 
HETATM 3931 O O     . HOH I 7 .   ? -36.067 -9.822  0.876   1.00 18.98 ? 812  HOH A O     1 
HETATM 3932 O O     . HOH I 7 .   ? -45.500 -13.198 1.506   1.00 37.79 ? 813  HOH A O     1 
HETATM 3933 O O     . HOH I 7 .   ? -31.887 -28.735 23.631  1.00 10.94 ? 814  HOH A O     1 
HETATM 3934 O O     . HOH I 7 .   ? -27.965 -28.670 31.147  1.00 15.64 ? 815  HOH A O     1 
HETATM 3935 O O     . HOH I 7 .   ? -24.514 -0.040  2.885   1.00 31.64 ? 816  HOH A O     1 
HETATM 3936 O O     . HOH I 7 .   ? -24.714 -10.514 37.828  1.00 33.52 ? 817  HOH A O     1 
HETATM 3937 O O     . HOH I 7 .   ? -22.472 -26.100 20.881  1.00 28.62 ? 818  HOH A O     1 
HETATM 3938 O O     . HOH I 7 .   ? -16.353 -25.148 36.434  1.00 33.63 ? 819  HOH A O     1 
HETATM 3939 O O     . HOH I 7 .   ? -31.107 -15.089 15.872  1.00 12.61 ? 820  HOH A O     1 
HETATM 3940 O O     . HOH I 7 .   ? -6.483  8.459   4.784   1.00 37.41 ? 821  HOH A O     1 
HETATM 3941 O O     . HOH I 7 .   ? -33.586 -9.933  2.098   1.00 16.54 ? 822  HOH A O     1 
HETATM 3942 O O     . HOH I 7 .   ? -18.765 10.069  29.010  1.00 27.64 ? 823  HOH A O     1 
HETATM 3943 O O     . HOH I 7 .   ? -7.067  -26.105 18.784  1.00 22.34 ? 824  HOH A O     1 
HETATM 3944 O O     . HOH I 7 .   ? -38.935 -14.901 27.584  1.00 30.27 ? 825  HOH A O     1 
HETATM 3945 O O     . HOH I 7 .   ? -47.368 -21.946 21.250  1.00 20.36 ? 826  HOH A O     1 
HETATM 3946 O O     . HOH I 7 .   ? -7.507  -16.180 -6.020  1.00 22.66 ? 827  HOH A O     1 
HETATM 3947 O O     . HOH I 7 .   ? -19.578 -31.216 -6.925  1.00 17.84 ? 828  HOH A O     1 
HETATM 3948 O O     . HOH I 7 .   ? -14.758 -24.063 -9.282  1.00 12.88 ? 829  HOH A O     1 
HETATM 3949 O O     . HOH I 7 .   ? -32.557 -25.714 34.356  0.50 13.52 ? 830  HOH A O     1 
HETATM 3950 O O     . HOH I 7 .   ? -5.272  -15.243 -3.338  1.00 22.10 ? 831  HOH A O     1 
HETATM 3951 O O     . HOH I 7 .   ? -22.803 -16.698 20.163  1.00 13.95 ? 832  HOH A O     1 
HETATM 3952 O O     . HOH I 7 .   ? -41.954 -19.542 26.898  1.00 22.27 ? 833  HOH A O     1 
HETATM 3953 O O     . HOH I 7 .   ? -32.577 -13.608 20.530  1.00 15.11 ? 834  HOH A O     1 
HETATM 3954 O O     . HOH I 7 .   ? -11.284 -26.424 15.250  1.00 30.60 ? 835  HOH A O     1 
HETATM 3955 O O     . HOH I 7 .   ? -19.602 -2.639  7.376   1.00 16.21 ? 836  HOH A O     1 
HETATM 3956 O O     . HOH I 7 .   ? -3.803  1.335   -0.275  1.00 43.78 ? 837  HOH A O     1 
HETATM 3957 O O     . HOH I 7 .   ? -12.712 -16.010 -2.779  1.00 19.07 ? 838  HOH A O     1 
HETATM 3958 O O     . HOH I 7 .   ? 1.063   -18.050 -2.247  1.00 34.98 ? 839  HOH A O     1 
HETATM 3959 O O     . HOH I 7 .   ? -23.798 2.025   4.037   1.00 30.21 ? 840  HOH A O     1 
HETATM 3960 O O     . HOH I 7 .   ? -1.655  -27.225 -2.087  1.00 30.51 ? 841  HOH A O     1 
HETATM 3961 O O     . HOH I 7 .   ? -30.270 -28.309 32.670  1.00 19.59 ? 842  HOH A O     1 
HETATM 3962 O O     . HOH I 7 .   ? -11.858 -22.546 23.341  1.00 15.79 ? 843  HOH A O     1 
HETATM 3963 O O     . HOH I 7 .   ? -37.864 -40.656 24.909  1.00 28.44 ? 844  HOH A O     1 
HETATM 3964 O O     . HOH I 7 .   ? -44.418 -37.240 11.814  1.00 21.02 ? 845  HOH A O     1 
HETATM 3965 O O     . HOH I 7 .   ? -22.337 -4.013  24.981  1.00 13.29 ? 846  HOH A O     1 
HETATM 3966 O O     . HOH I 7 .   ? -30.182 -30.525 22.482  1.00 15.00 ? 847  HOH A O     1 
HETATM 3967 O O     . HOH I 7 .   ? -43.610 -39.594 24.559  1.00 26.64 ? 848  HOH A O     1 
HETATM 3968 O O     . HOH I 7 .   ? -16.218 6.186   22.909  1.00 15.94 ? 849  HOH A O     1 
HETATM 3969 O O     . HOH I 7 .   ? -38.198 -1.004  9.911   1.00 20.65 ? 850  HOH A O     1 
HETATM 3970 O O     . HOH I 7 .   ? -22.113 -11.029 23.319  1.00 24.15 ? 851  HOH A O     1 
HETATM 3971 O O     . HOH I 7 .   ? -25.631 -34.935 -2.331  1.00 42.57 ? 852  HOH A O     1 
HETATM 3972 O O     . HOH I 7 .   ? -26.965 -23.606 23.537  1.00 12.38 ? 853  HOH A O     1 
HETATM 3973 O O     . HOH I 7 .   ? -4.769  -26.694 8.931   1.00 17.53 ? 854  HOH A O     1 
HETATM 3974 O O     . HOH I 7 .   ? -48.988 -27.835 28.052  1.00 41.42 ? 855  HOH A O     1 
HETATM 3975 O O     . HOH I 7 .   ? -39.248 -38.271 31.341  1.00 33.83 ? 856  HOH A O     1 
HETATM 3976 O O     . HOH I 7 .   ? -23.942 1.098   15.683  1.00 14.46 ? 857  HOH A O     1 
HETATM 3977 O O     . HOH I 7 .   ? -38.130 -8.894  28.835  1.00 31.69 ? 858  HOH A O     1 
HETATM 3978 O O     . HOH I 7 .   ? -22.983 -19.784 -6.814  1.00 25.60 ? 859  HOH A O     1 
HETATM 3979 O O     . HOH I 7 .   ? -33.237 0.137   7.917   1.00 26.32 ? 860  HOH A O     1 
HETATM 3980 O O     . HOH I 7 .   ? -11.931 -8.281  9.204   1.00 14.93 ? 861  HOH A O     1 
HETATM 3981 O O     . HOH I 7 .   ? -9.394  8.457   18.328  1.00 20.01 ? 862  HOH A O     1 
HETATM 3982 O O     . HOH I 7 .   ? -6.309  -22.418 -2.861  1.00 28.11 ? 863  HOH A O     1 
HETATM 3983 O O     . HOH I 7 .   ? -28.303 -19.141 35.867  1.00 32.09 ? 864  HOH A O     1 
HETATM 3984 O O     . HOH I 7 .   ? -24.370 5.239   15.330  1.00 17.22 ? 865  HOH A O     1 
HETATM 3985 O O     . HOH I 7 .   ? -14.947 -23.983 1.727   1.00 13.57 ? 866  HOH A O     1 
HETATM 3986 O O     . HOH I 7 .   ? -27.344 1.234   4.476   1.00 29.37 ? 867  HOH A O     1 
HETATM 3987 O O     . HOH I 7 .   ? -17.139 -3.559  -2.494  1.00 34.54 ? 868  HOH A O     1 
HETATM 3988 O O     . HOH I 7 .   ? 0.145   -16.261 10.954  1.00 31.98 ? 869  HOH A O     1 
HETATM 3989 O O     . HOH I 7 .   ? -7.672  7.887   9.822   1.00 26.23 ? 870  HOH A O     1 
HETATM 3990 O O     . HOH I 7 .   ? -6.148  -4.104  40.005  1.00 23.83 ? 871  HOH A O     1 
HETATM 3991 O O     . HOH I 7 .   ? 7.536   -9.164  27.003  1.00 27.67 ? 872  HOH A O     1 
HETATM 3992 O O     . HOH I 7 .   ? -26.213 8.052   16.991  1.00 24.36 ? 873  HOH A O     1 
HETATM 3993 O O     . HOH I 7 .   ? -15.684 -23.787 -12.059 1.00 18.72 ? 874  HOH A O     1 
HETATM 3994 O O     . HOH I 7 .   ? -28.814 -9.709  12.208  1.00 13.90 ? 875  HOH A O     1 
HETATM 3995 O O     . HOH I 7 .   ? -9.475  -27.311 12.987  1.00 19.60 ? 876  HOH A O     1 
HETATM 3996 O O     . HOH I 7 .   ? -26.013 2.037   11.655  1.00 21.29 ? 877  HOH A O     1 
HETATM 3997 O O     . HOH I 7 .   ? -12.486 -3.242  40.680  1.00 25.96 ? 878  HOH A O     1 
HETATM 3998 O O     . HOH I 7 .   ? -7.905  6.282   16.345  1.00 15.52 ? 879  HOH A O     1 
HETATM 3999 O O     . HOH I 7 .   ? -36.596 -41.111 13.648  1.00 31.32 ? 880  HOH A O     1 
HETATM 4000 O O     . HOH I 7 .   ? -18.634 -23.085 40.467  1.00 32.45 ? 881  HOH A O     1 
HETATM 4001 O O     . HOH I 7 .   ? -22.961 -1.808  29.895  1.00 24.35 ? 882  HOH A O     1 
HETATM 4002 O O     . HOH I 7 .   ? -15.228 -25.406 29.740  1.00 26.87 ? 883  HOH A O     1 
HETATM 4003 O O     . HOH I 7 .   ? -23.545 -15.142 30.903  1.00 12.69 ? 884  HOH A O     1 
HETATM 4004 O O     . HOH I 7 .   ? -19.974 -24.483 -13.885 1.00 38.76 ? 885  HOH A O     1 
HETATM 4005 O O     . HOH I 7 .   ? -24.222 -15.102 28.276  1.00 13.98 ? 886  HOH A O     1 
HETATM 4006 O O     . HOH I 7 .   ? -14.756 -18.815 3.756   1.00 14.51 ? 887  HOH A O     1 
HETATM 4007 O O     . HOH I 7 .   ? -29.416 -0.462  22.491  1.00 26.13 ? 888  HOH A O     1 
HETATM 4008 O O     . HOH I 7 .   ? -41.618 -37.380 33.792  1.00 44.77 ? 889  HOH A O     1 
HETATM 4009 O O     . HOH I 7 .   ? -14.112 -5.853  -1.060  1.00 27.81 ? 890  HOH A O     1 
HETATM 4010 O O     . HOH I 7 .   ? -43.694 -22.230 26.198  1.00 16.95 ? 891  HOH A O     1 
HETATM 4011 O O     . HOH I 7 .   ? -23.744 11.594  20.265  1.00 32.32 ? 892  HOH A O     1 
HETATM 4012 O O     . HOH I 7 .   ? -11.537 9.396   10.865  1.00 37.59 ? 893  HOH A O     1 
HETATM 4013 O O     . HOH I 7 .   ? -10.943 -30.853 2.248   1.00 30.00 ? 894  HOH A O     1 
HETATM 4014 O O     . HOH I 7 .   ? -23.767 -32.782 -5.033  1.00 27.20 ? 895  HOH A O     1 
HETATM 4015 O O     . HOH I 7 .   ? -5.501  -19.605 9.313   1.00 24.17 ? 896  HOH A O     1 
HETATM 4016 O O     . HOH I 7 .   ? -48.086 -33.081 14.869  1.00 16.49 ? 897  HOH A O     1 
HETATM 4017 O O     . HOH I 7 .   ? -15.958 -19.901 -10.611 1.00 25.89 ? 898  HOH A O     1 
HETATM 4018 O O     . HOH I 7 .   ? -15.315 -15.952 21.419  1.00 32.38 ? 899  HOH A O     1 
HETATM 4019 O O     . HOH I 7 .   ? -23.769 -32.642 25.725  1.00 39.38 ? 900  HOH A O     1 
HETATM 4020 O O     . HOH I 7 .   ? -52.425 -19.652 10.485  1.00 23.63 ? 901  HOH A O     1 
HETATM 4021 O O     . HOH I 7 .   ? -27.853 -34.116 18.813  1.00 24.40 ? 902  HOH A O     1 
HETATM 4022 O O     . HOH I 7 .   ? -19.204 -34.252 -1.208  1.00 32.49 ? 903  HOH A O     1 
HETATM 4023 O O     . HOH I 7 .   ? -18.733 -34.321 7.241   1.00 31.83 ? 904  HOH A O     1 
HETATM 4024 O O     . HOH I 7 .   ? 11.073  -8.799  19.841  1.00 47.22 ? 905  HOH A O     1 
HETATM 4025 O O     . HOH I 7 .   ? -24.116 -16.941 37.524  1.00 41.31 ? 906  HOH A O     1 
HETATM 4026 O O     . HOH I 7 .   ? -9.815  -17.466 -6.930  1.00 26.88 ? 907  HOH A O     1 
HETATM 4027 O O     . HOH I 7 .   ? -21.307 5.748   8.445   1.00 35.12 ? 908  HOH A O     1 
HETATM 4028 O O     . HOH I 7 .   ? 4.289   -19.715 5.053   1.00 28.98 ? 909  HOH A O     1 
HETATM 4029 O O     . HOH I 7 .   ? -47.107 -22.870 2.186   1.00 36.87 ? 910  HOH A O     1 
HETATM 4030 O O     . HOH I 7 .   ? -23.121 -35.422 9.332   1.00 42.04 ? 911  HOH A O     1 
HETATM 4031 O O     . HOH I 7 .   ? -51.345 -12.603 11.256  1.00 43.62 ? 912  HOH A O     1 
HETATM 4032 O O     . HOH I 7 .   ? -30.943 -29.660 -5.321  1.00 40.53 ? 913  HOH A O     1 
HETATM 4033 O O     . HOH I 7 .   ? -12.491 -17.244 37.393  1.00 17.51 ? 914  HOH A O     1 
HETATM 4034 O O     . HOH I 7 .   ? -28.788 -26.330 30.111  1.00 16.23 ? 915  HOH A O     1 
HETATM 4035 O O     . HOH I 7 .   ? -34.599 -20.121 29.291  1.00 17.73 ? 916  HOH A O     1 
HETATM 4036 O O     . HOH I 7 .   ? -14.806 -3.624  -1.241  1.00 38.54 ? 917  HOH A O     1 
HETATM 4037 O O     . HOH I 7 .   ? 2.593   -6.639  6.386   1.00 27.46 ? 918  HOH A O     1 
HETATM 4038 O O     . HOH I 7 .   ? -31.074 1.954   1.368   1.00 30.00 ? 919  HOH A O     1 
HETATM 4039 O O     . HOH I 7 .   ? -13.202 -0.441  5.754   1.00 25.50 ? 920  HOH A O     1 
HETATM 4040 O O     . HOH I 7 .   ? -5.914  -10.880 16.386  1.00 30.51 ? 921  HOH A O     1 
HETATM 4041 O O     . HOH I 7 .   ? -17.155 8.947   19.829  1.00 22.91 ? 922  HOH A O     1 
HETATM 4042 O O     . HOH I 7 .   ? -50.545 -20.344 17.368  1.00 23.00 ? 923  HOH A O     1 
HETATM 4043 O O     . HOH I 7 .   ? -14.297 -0.448  3.660   1.00 33.03 ? 924  HOH A O     1 
HETATM 4044 O O     . HOH I 7 .   ? 2.305   -11.576 26.389  1.00 28.95 ? 925  HOH A O     1 
HETATM 4045 O O     . HOH I 7 .   ? -34.395 -42.379 31.804  1.00 24.35 ? 926  HOH A O     1 
HETATM 4046 O O     . HOH I 7 .   ? -14.384 -0.642  8.280   1.00 20.20 ? 927  HOH A O     1 
HETATM 4047 O O     . HOH I 7 .   ? -42.553 -5.402  4.903   1.00 30.91 ? 928  HOH A O     1 
HETATM 4048 O O     . HOH I 7 .   ? -27.187 -31.114 20.867  1.00 26.31 ? 929  HOH A O     1 
HETATM 4049 O O     . HOH I 7 .   ? -23.053 2.012   26.840  1.00 32.51 ? 930  HOH A O     1 
HETATM 4050 O O     . HOH I 7 .   ? -36.072 -24.454 23.330  1.00 35.01 ? 931  HOH A O     1 
HETATM 4051 O O     . HOH I 7 .   ? -27.106 -16.814 18.547  1.00 10.84 ? 932  HOH A O     1 
HETATM 4052 O O     . HOH I 7 .   ? -49.642 -21.197 14.847  1.00 17.10 ? 933  HOH A O     1 
HETATM 4053 O O     . HOH I 7 .   ? -10.163 -11.014 39.420  1.00 17.61 ? 934  HOH A O     1 
HETATM 4054 O O     . HOH I 7 .   ? -23.161 -34.842 0.576   1.00 41.87 ? 935  HOH A O     1 
HETATM 4055 O O     . HOH I 7 .   ? -28.937 -25.073 27.678  1.00 19.29 ? 936  HOH A O     1 
HETATM 4056 O O     . HOH I 7 .   ? -14.653 -16.420 5.519   1.00 15.96 ? 937  HOH A O     1 
HETATM 4057 O O     . HOH I 7 .   ? -8.533  1.252   5.608   1.00 17.63 ? 938  HOH A O     1 
HETATM 4058 O O     . HOH I 7 .   ? -7.780  5.886   1.628   1.00 19.61 ? 939  HOH A O     1 
HETATM 4059 O O     . HOH I 7 .   ? -43.588 -20.872 -0.727  1.00 22.82 ? 940  HOH A O     1 
HETATM 4060 O O     . HOH I 7 .   ? -15.347 -9.084  8.842   1.00 25.05 ? 941  HOH A O     1 
HETATM 4061 O O     . HOH I 7 .   ? -27.655 2.214   21.307  1.00 22.38 ? 942  HOH A O     1 
HETATM 4062 O O     . HOH I 7 .   ? -20.651 -33.525 -10.020 1.00 47.34 ? 943  HOH A O     1 
HETATM 4063 O O     . HOH I 7 .   ? -25.991 -16.928 35.566  1.00 23.30 ? 944  HOH A O     1 
HETATM 4064 O O     . HOH I 7 .   ? -27.146 -7.950  14.713  1.00 20.70 ? 945  HOH A O     1 
HETATM 4065 O O     . HOH I 7 .   ? -25.344 -15.876 20.658  1.00 11.72 ? 946  HOH A O     1 
HETATM 4066 O O     . HOH I 7 .   ? -13.227 10.190  27.919  1.00 30.07 ? 947  HOH A O     1 
HETATM 4067 O O     . HOH I 7 .   ? -15.630 11.411  10.284  1.00 36.20 ? 948  HOH A O     1 
HETATM 4068 O O     . HOH I 7 .   ? -34.824 -16.041 30.036  1.00 27.59 ? 949  HOH A O     1 
HETATM 4069 O O     . HOH I 7 .   ? 3.029   -16.575 -0.873  1.00 32.63 ? 950  HOH A O     1 
HETATM 4070 O O     . HOH I 7 .   ? -5.714  -25.715 -3.075  1.00 35.90 ? 951  HOH A O     1 
HETATM 4071 O O     . HOH I 7 .   ? -16.870 2.745   8.162   1.00 38.02 ? 952  HOH A O     1 
HETATM 4072 O O     . HOH I 7 .   ? -39.900 -33.428 4.726   1.00 15.00 ? 953  HOH A O     1 
HETATM 4073 O O     . HOH I 7 .   ? -27.494 1.173   9.523   1.00 23.57 ? 954  HOH A O     1 
HETATM 4074 O O     . HOH I 7 .   ? -41.818 -11.181 -2.682  1.00 29.63 ? 955  HOH A O     1 
HETATM 4075 O O     . HOH I 7 .   ? -30.776 -34.086 33.972  1.00 17.67 ? 956  HOH A O     1 
HETATM 4076 O O     . HOH I 7 .   ? -36.687 -1.649  21.716  1.00 31.23 ? 957  HOH A O     1 
HETATM 4077 O O     . HOH I 7 .   ? -6.527  -9.320  1.129   1.00 30.09 ? 958  HOH A O     1 
HETATM 4078 O O     . HOH I 7 .   ? -25.179 -32.164 32.696  1.00 33.18 ? 959  HOH A O     1 
HETATM 4079 O O     . HOH I 7 .   ? -38.394 -41.071 10.927  1.00 30.64 ? 960  HOH A O     1 
HETATM 4080 O O     . HOH I 7 .   ? 6.439   -16.005 10.608  1.00 37.52 ? 961  HOH A O     1 
HETATM 4081 O O     . HOH I 7 .   ? -13.138 -9.780  6.886   1.00 14.69 ? 962  HOH A O     1 
HETATM 4082 O O     . HOH I 7 .   ? -43.216 -12.934 3.103   1.00 19.99 ? 963  HOH A O     1 
HETATM 4083 O O     . HOH I 7 .   ? -39.652 -27.648 31.214  1.00 17.82 ? 964  HOH A O     1 
HETATM 4084 O O     . HOH I 7 .   ? -26.909 -1.621  -1.675  1.00 30.00 ? 965  HOH A O     1 
HETATM 4085 O O     . HOH I 7 .   ? -4.796  -24.304 24.287  1.00 46.07 ? 966  HOH A O     1 
HETATM 4086 O O     . HOH I 7 .   ? -17.696 -13.874 17.977  1.00 39.51 ? 967  HOH A O     1 
HETATM 4087 O O     . HOH I 7 .   ? -23.172 -33.387 14.108  1.00 44.88 ? 968  HOH A O     1 
HETATM 4088 O O     . HOH I 7 .   ? -37.259 -20.068 15.225  1.00 17.50 ? 969  HOH A O     1 
HETATM 4089 O O     . HOH I 7 .   ? -37.490 0.493   13.752  1.00 24.40 ? 970  HOH A O     1 
HETATM 4090 O O     . HOH I 7 .   ? -6.403  8.441   17.031  1.00 28.08 ? 971  HOH A O     1 
HETATM 4091 O O     . HOH I 7 .   ? -25.729 -3.657  27.559  1.00 21.04 ? 972  HOH A O     1 
HETATM 4092 O O     . HOH I 7 .   ? -37.014 -4.134  28.323  1.00 22.08 ? 973  HOH A O     1 
HETATM 4093 O O     . HOH I 7 .   ? -33.732 -20.427 31.962  1.00 30.37 ? 974  HOH A O     1 
HETATM 4094 O O     . HOH I 7 .   ? -18.927 -13.222 16.103  1.00 39.67 ? 975  HOH A O     1 
HETATM 4095 O O     . HOH I 7 .   ? -6.595  10.878  16.960  1.00 32.01 ? 976  HOH A O     1 
HETATM 4096 O O     . HOH I 7 .   ? -31.185 -15.732 19.411  1.00 12.72 ? 977  HOH A O     1 
HETATM 4097 O O     . HOH I 7 .   ? -37.004 2.358   9.524   1.00 43.44 ? 978  HOH A O     1 
HETATM 4098 O O     . HOH I 7 .   ? -49.919 -32.013 27.131  1.00 35.48 ? 979  HOH A O     1 
HETATM 4099 O O     . HOH I 7 .   ? 9.719   0.064   18.536  1.00 33.05 ? 980  HOH A O     1 
HETATM 4100 O O     . HOH I 7 .   ? -28.100 -40.172 26.953  1.00 29.91 ? 981  HOH A O     1 
HETATM 4101 O O     . HOH I 7 .   ? -50.002 -16.283 10.197  1.00 32.70 ? 982  HOH A O     1 
HETATM 4102 O O     . HOH I 7 .   ? -27.229 -2.726  29.812  1.00 26.67 ? 983  HOH A O     1 
HETATM 4103 O O     . HOH I 7 .   ? -26.418 -35.135 1.733   1.00 26.60 ? 984  HOH A O     1 
HETATM 4104 O O     . HOH I 7 .   ? -3.030  -12.556 28.543  1.00 29.28 ? 985  HOH A O     1 
HETATM 4105 O O     . HOH I 7 .   ? -6.773  -15.899 24.644  1.00 31.21 ? 986  HOH A O     1 
HETATM 4106 O O     . HOH I 7 .   ? -22.073 -23.060 -16.143 1.00 48.40 ? 987  HOH A O     1 
HETATM 4107 O O     . HOH I 7 .   ? 10.137  -8.825  22.708  1.00 51.37 ? 988  HOH A O     1 
HETATM 4108 O O     . HOH I 7 .   ? -44.378 -13.573 -3.057  1.00 35.28 ? 989  HOH A O     1 
HETATM 4109 O O     . HOH I 7 .   ? -17.718 -29.140 14.048  1.00 26.68 ? 990  HOH A O     1 
HETATM 4110 O O     . HOH I 7 .   ? -28.295 -37.085 9.215   1.00 42.48 ? 991  HOH A O     1 
HETATM 4111 O O     . HOH I 7 .   ? -16.872 -22.387 3.002   1.00 14.91 ? 992  HOH A O     1 
HETATM 4112 O O     . HOH I 7 .   ? -29.121 6.774   20.499  1.00 43.00 ? 993  HOH A O     1 
HETATM 4113 O O     . HOH I 7 .   ? 1.158   -2.163  34.230  1.00 25.83 ? 994  HOH A O     1 
HETATM 4114 O O     . HOH I 7 .   ? 3.065   -8.732  30.317  1.00 30.99 ? 995  HOH A O     1 
HETATM 4115 O O     . HOH I 7 .   ? -45.993 -18.987 0.240   1.00 27.83 ? 996  HOH A O     1 
HETATM 4116 O O     . HOH I 7 .   ? 2.492   1.193   19.022  1.00 23.13 ? 997  HOH A O     1 
HETATM 4117 O O     . HOH I 7 .   ? -41.503 -44.926 11.831  1.00 43.71 ? 998  HOH A O     1 
HETATM 4118 O O     . HOH I 7 .   ? -17.905 -29.433 11.457  1.00 22.98 ? 999  HOH A O     1 
HETATM 4119 O O     . HOH I 7 .   ? -47.345 -35.558 15.644  1.00 20.26 ? 1000 HOH A O     1 
HETATM 4120 O O     . HOH I 7 .   ? -18.077 -18.584 13.753  1.00 23.39 ? 1001 HOH A O     1 
HETATM 4121 O O     . HOH I 7 .   ? -12.276 -11.690 14.513  1.00 43.24 ? 1002 HOH A O     1 
HETATM 4122 O O     . HOH I 7 .   ? -51.849 -26.464 11.683  1.00 41.33 ? 1003 HOH A O     1 
HETATM 4123 O O     . HOH I 7 .   ? -43.542 -10.799 1.084   1.00 24.16 ? 1004 HOH A O     1 
HETATM 4124 O O     . HOH I 7 .   ? 2.926   -16.526 19.842  1.00 46.71 ? 1005 HOH A O     1 
HETATM 4125 O O     . HOH I 7 .   ? -13.900 -9.564  -4.094  1.00 44.24 ? 1006 HOH A O     1 
HETATM 4126 O O     . HOH I 7 .   ? -35.663 -32.327 5.181   1.00 28.96 ? 1007 HOH A O     1 
HETATM 4127 O O     . HOH I 7 .   ? -13.768 -28.360 18.725  1.00 44.73 ? 1008 HOH A O     1 
HETATM 4128 O O     . HOH I 7 .   ? -28.004 -35.421 6.951   1.00 24.34 ? 1009 HOH A O     1 
HETATM 4129 O O     . HOH I 7 .   ? -23.034 -26.775 23.276  1.00 34.74 ? 1010 HOH A O     1 
HETATM 4130 O O     . HOH I 7 .   ? -26.291 -10.989 36.056  1.00 26.19 ? 1011 HOH A O     1 
HETATM 4131 O O     . HOH I 7 .   ? -1.972  -25.108 2.892   1.00 24.92 ? 1012 HOH A O     1 
HETATM 4132 O O     . HOH I 7 .   ? -20.221 0.000   0.000   0.50 38.03 ? 1013 HOH A O     1 
HETATM 4133 O O     . HOH I 7 .   ? 4.042   -3.460  24.083  1.00 42.11 ? 1014 HOH A O     1 
HETATM 4134 O O     . HOH I 7 .   ? -15.691 -16.058 38.979  1.00 37.90 ? 1015 HOH A O     1 
HETATM 4135 O O     . HOH I 7 .   ? -3.684  6.121   10.453  1.00 26.48 ? 1016 HOH A O     1 
HETATM 4136 O O     . HOH I 7 .   ? -14.253 -30.659 8.465   1.00 37.15 ? 1017 HOH A O     1 
HETATM 4137 O O     . HOH I 7 .   ? -22.444 -7.595  43.901  1.00 39.84 ? 1018 HOH A O     1 
HETATM 4138 O O     . HOH I 7 .   ? -6.847  12.616  25.882  1.00 44.54 ? 1019 HOH A O     1 
HETATM 4139 O O     . HOH I 7 .   ? -29.400 2.956   8.470   1.00 31.48 ? 1020 HOH A O     1 
HETATM 4140 O O     . HOH I 7 .   ? -37.585 -16.861 26.990  1.00 32.12 ? 1021 HOH A O     1 
HETATM 4141 O O     . HOH I 7 .   ? -13.419 2.041   8.084   1.00 30.00 ? 1022 HOH A O     1 
HETATM 4142 O O     . HOH I 7 .   ? -3.977  -13.459 15.477  1.00 29.94 ? 1023 HOH A O     1 
HETATM 4143 O O     . HOH I 7 .   ? -21.758 -11.724 -4.343  1.00 31.84 ? 1024 HOH A O     1 
HETATM 4144 O O     . HOH I 7 .   ? -10.007 -32.705 4.259   1.00 41.51 ? 1025 HOH A O     1 
HETATM 4145 O O     . HOH I 7 .   ? -25.240 -0.339  24.147  1.00 27.83 ? 1026 HOH A O     1 
HETATM 4146 O O     . HOH I 7 .   ? -25.316 -34.099 24.029  1.00 32.46 ? 1027 HOH A O     1 
HETATM 4147 O O     . HOH I 7 .   ? -41.489 -32.851 34.138  1.00 41.05 ? 1028 HOH A O     1 
HETATM 4148 O O     . HOH I 7 .   ? -8.105  -30.194 2.008   1.00 26.23 ? 1029 HOH A O     1 
HETATM 4149 O O     . HOH I 7 .   ? -19.919 -26.038 20.506  1.00 28.08 ? 1030 HOH A O     1 
HETATM 4150 O O     . HOH I 7 .   ? -43.531 -15.322 25.832  1.00 25.87 ? 1031 HOH A O     1 
HETATM 4151 O O     . HOH I 7 .   ? -3.562  -19.740 22.446  1.00 39.40 ? 1032 HOH A O     1 
HETATM 4152 O O     . HOH I 7 .   ? -9.634  6.946   14.368  1.00 26.13 ? 1033 HOH A O     1 
HETATM 4153 O O     . HOH I 7 .   ? -50.454 -32.839 15.907  1.00 28.62 ? 1034 HOH A O     1 
HETATM 4154 O O     . HOH I 7 .   ? -31.119 -19.677 31.718  1.00 32.07 ? 1035 HOH A O     1 
HETATM 4155 O O     . HOH I 7 .   ? -38.074 2.409   12.011  1.00 37.83 ? 1036 HOH A O     1 
HETATM 4156 O O     . HOH I 7 .   ? -35.727 1.127   7.892   1.00 40.10 ? 1037 HOH A O     1 
HETATM 4157 O O     . HOH I 7 .   ? -4.032  -23.462 17.076  1.00 34.50 ? 1038 HOH A O     1 
HETATM 4158 O O     . HOH I 7 .   ? -8.827  -19.824 38.006  1.00 31.13 ? 1039 HOH A O     1 
HETATM 4159 O O     . HOH I 7 .   ? -23.642 -31.092 27.615  1.00 33.42 ? 1040 HOH A O     1 
HETATM 4160 O O     . HOH I 7 .   ? -22.572 -36.946 30.718  1.00 46.02 ? 1041 HOH A O     1 
HETATM 4161 O O     . HOH I 7 .   ? -25.423 0.000   0.000   0.50 44.49 ? 1042 HOH A O     1 
HETATM 4162 O O     . HOH I 7 .   ? -34.125 -26.312 -4.336  1.00 42.73 ? 1043 HOH A O     1 
HETATM 4163 O O     . HOH I 7 .   ? -34.217 -42.725 24.452  1.00 31.19 ? 1044 HOH A O     1 
HETATM 4164 O O     . HOH I 7 .   ? 2.621   4.613   25.655  1.00 35.88 ? 1045 HOH A O     1 
HETATM 4165 O O     . HOH I 7 .   ? -13.584 10.714  25.242  1.00 29.34 ? 1046 HOH A O     1 
HETATM 4166 O O     . HOH I 7 .   ? -41.622 -11.442 22.719  1.00 25.71 ? 1047 HOH A O     1 
HETATM 4167 O O     . HOH I 7 .   ? -40.344 -20.557 -4.530  1.00 41.55 ? 1048 HOH A O     1 
HETATM 4168 O O     . HOH I 7 .   ? -9.422  2.938   35.272  1.00 37.79 ? 1049 HOH A O     1 
HETATM 4169 O O     . HOH I 7 .   ? -13.220 -22.931 30.704  1.00 36.47 ? 1050 HOH A O     1 
HETATM 4170 O O     . HOH I 7 .   ? -18.234 -25.114 38.578  1.00 48.88 ? 1051 HOH A O     1 
HETATM 4171 O O     . HOH I 7 .   ? -45.565 -42.647 18.282  1.00 22.32 ? 1052 HOH A O     1 
HETATM 4172 O O     . HOH I 7 .   ? -26.158 1.487   7.063   1.00 33.69 ? 1053 HOH A O     1 
HETATM 4173 O O     . HOH I 7 .   ? -13.184 10.507  17.632  1.00 34.21 ? 1054 HOH A O     1 
HETATM 4174 O O     . HOH I 7 .   ? -5.232  -26.856 11.730  1.00 25.84 ? 1055 HOH A O     1 
HETATM 4175 O O     . HOH I 7 .   ? -24.264 -30.673 30.606  1.00 40.55 ? 1056 HOH A O     1 
HETATM 4176 O O     . HOH I 7 .   ? -30.365 -40.780 26.196  1.00 35.92 ? 1057 HOH A O     1 
HETATM 4177 O O     . HOH I 7 .   ? -36.545 5.308   12.445  1.00 62.35 ? 1058 HOH A O     1 
HETATM 4178 O O     . HOH I 7 .   ? -30.740 2.707   15.017  1.00 36.44 ? 1059 HOH A O     1 
HETATM 4179 O O     . HOH I 7 .   ? -37.413 -45.989 15.660  1.00 40.66 ? 1060 HOH A O     1 
HETATM 4180 O O     . HOH I 7 .   ? -42.460 -22.038 -3.700  1.00 37.29 ? 1061 HOH A O     1 
HETATM 4181 O O     . HOH I 7 .   ? -2.493  -21.873 22.804  1.00 47.38 ? 1062 HOH A O     1 
HETATM 4182 O O     . HOH I 7 .   ? -43.265 -23.004 -1.560  1.00 36.34 ? 1063 HOH A O     1 
HETATM 4183 O O     . HOH I 7 .   ? -17.060 5.164   31.506  1.00 41.01 ? 1064 HOH A O     1 
HETATM 4184 O O     . HOH I 7 .   ? -7.514  -26.467 21.548  1.00 31.64 ? 1065 HOH A O     1 
HETATM 4185 O O     . HOH I 7 .   ? -47.316 -42.153 22.866  1.00 33.14 ? 1066 HOH A O     1 
HETATM 4186 O O     . HOH I 7 .   ? -17.926 -12.711 22.408  1.00 34.98 ? 1067 HOH A O     1 
HETATM 4187 O O     . HOH I 7 .   ? -24.146 -2.155  25.905  1.00 17.25 ? 1068 HOH A O     1 
HETATM 4188 O O     . HOH I 7 .   ? 1.594   -3.607  25.064  1.00 27.73 ? 1069 HOH A O     1 
HETATM 4189 O O     . HOH I 7 .   ? -39.489 -18.083 28.006  1.00 30.00 ? 1070 HOH A O     1 
HETATM 4190 O O     . HOH I 7 .   ? -10.007 -17.420 38.152  1.00 27.38 ? 1071 HOH A O     1 
HETATM 4191 O O     . HOH I 7 .   ? -16.972 -26.517 34.124  1.00 38.56 ? 1072 HOH A O     1 
HETATM 4192 O O     . HOH I 7 .   ? -51.531 -32.687 20.830  1.00 30.95 ? 1073 HOH A O     1 
HETATM 4193 O O     . HOH I 7 .   ? -5.101  -6.867  -1.855  1.00 33.18 ? 1074 HOH A O     1 
HETATM 4194 O O     . HOH I 7 .   ? -53.096 -26.200 26.443  1.00 49.04 ? 1075 HOH A O     1 
HETATM 4195 O O     . HOH I 7 .   ? -33.467 -17.706 28.218  1.00 23.81 ? 1076 HOH A O     1 
HETATM 4196 O O     . HOH I 7 .   ? -16.331 -11.325 13.175  1.00 31.72 ? 1077 HOH A O     1 
HETATM 4197 O O     . HOH I 7 .   ? 2.076   0.368   33.383  1.00 20.27 ? 1078 HOH A O     1 
HETATM 4198 O O     . HOH I 7 .   ? -44.035 -39.534 11.120  1.00 32.83 ? 1079 HOH A O     1 
HETATM 4199 O O     . HOH I 7 .   ? -49.383 -19.021 13.270  1.00 18.78 ? 1080 HOH A O     1 
HETATM 4200 O O     . HOH I 7 .   ? -4.315  2.008   34.767  1.00 31.06 ? 1081 HOH A O     1 
HETATM 4201 O O     . HOH I 7 .   ? -7.869  -13.991 -3.888  1.00 33.08 ? 1082 HOH A O     1 
HETATM 4202 O O     . HOH I 7 .   ? -9.345  -27.465 16.682  1.00 41.22 ? 1083 HOH A O     1 
HETATM 4203 O O     . HOH I 7 .   ? -27.583 -35.379 21.054  1.00 32.15 ? 1084 HOH A O     1 
HETATM 4204 O O     . HOH I 7 .   ? -12.296 -19.402 8.054   1.00 20.92 ? 1085 HOH A O     1 
HETATM 4205 O O     . HOH I 7 .   ? -12.512 -11.605 -4.875  1.00 37.54 ? 1086 HOH A O     1 
HETATM 4206 O O     . HOH I 7 .   ? -4.274  -25.810 18.104  1.00 37.14 ? 1087 HOH A O     1 
HETATM 4207 O O     . HOH I 7 .   ? 7.696   -3.032  23.608  1.00 41.10 ? 1088 HOH A O     1 
HETATM 4208 O O     . HOH I 7 .   ? -26.188 4.433   13.201  1.00 29.46 ? 1089 HOH A O     1 
HETATM 4209 O O     . HOH I 7 .   ? -45.605 -41.002 24.880  1.00 32.97 ? 1090 HOH A O     1 
HETATM 4210 O O     . HOH I 7 .   ? -39.924 0.220   8.645   1.00 39.32 ? 1091 HOH A O     1 
HETATM 4211 O O     . HOH I 7 .   ? 9.310   -9.321  15.035  1.00 49.18 ? 1092 HOH A O     1 
HETATM 4212 O O     . HOH I 7 .   ? -51.063 -25.435 14.056  1.00 21.00 ? 1093 HOH A O     1 
HETATM 4213 O O     . HOH I 7 .   ? -26.425 -37.726 27.146  1.00 25.69 ? 1094 HOH A O     1 
HETATM 4214 O O     . HOH I 7 .   ? -4.820  -18.538 30.824  1.00 30.00 ? 1095 HOH A O     1 
HETATM 4215 O O     . HOH I 7 .   ? -25.552 -29.245 32.447  1.00 24.54 ? 1096 HOH A O     1 
HETATM 4216 O O     . HOH I 7 .   ? -6.955  -28.447 12.924  1.00 34.16 ? 1097 HOH A O     1 
HETATM 4217 O O     . HOH I 7 .   ? -6.807  -17.187 11.464  1.00 40.99 ? 1098 HOH A O     1 
HETATM 4218 O O     . HOH I 7 .   ? -1.087  -15.566 -5.082  1.00 37.07 ? 1099 HOH A O     1 
HETATM 4219 O O     . HOH I 7 .   ? -10.380 -14.817 -3.681  1.00 28.41 ? 1100 HOH A O     1 
HETATM 4220 O O     . HOH I 7 .   ? -4.322  5.875   7.470   1.00 31.86 ? 1101 HOH A O     1 
HETATM 4221 O O     . HOH I 7 .   ? -48.667 0.664   8.835   1.00 54.52 ? 1102 HOH A O     1 
HETATM 4222 O O     . HOH I 7 .   ? 1.389   -13.208 24.033  1.00 41.43 ? 1103 HOH A O     1 
HETATM 4223 O O     . HOH I 7 .   ? -16.452 -6.093  41.458  1.00 53.63 ? 1104 HOH A O     1 
HETATM 4224 O O     . HOH I 7 .   ? -32.439 2.582   16.411  1.00 37.78 ? 1105 HOH A O     1 
HETATM 4225 O O     . HOH I 7 .   ? -47.085 -36.449 12.636  1.00 26.98 ? 1106 HOH A O     1 
HETATM 4226 O O     . HOH I 7 .   ? -17.849 12.177  13.390  1.00 41.15 ? 1107 HOH A O     1 
HETATM 4227 O O     . HOH I 7 .   ? 6.126   -10.448 28.662  1.00 29.07 ? 1108 HOH A O     1 
HETATM 4228 O O     . HOH I 7 .   ? -4.474  8.782   30.466  1.00 46.76 ? 1109 HOH A O     1 
HETATM 4229 O O     . HOH I 7 .   ? -15.043 -10.424 11.126  1.00 36.15 ? 1110 HOH A O     1 
HETATM 4230 O O     . HOH I 7 .   ? 3.269   -1.532  22.805  1.00 41.64 ? 1111 HOH A O     1 
HETATM 4231 O O     . HOH I 7 .   ? -15.434 -27.213 21.129  1.00 30.85 ? 1112 HOH A O     1 
HETATM 4232 O O     . HOH I 7 .   ? -53.755 -31.783 22.319  1.00 38.36 ? 1113 HOH A O     1 
HETATM 4233 O O     . HOH I 7 .   ? -23.313 -0.268  27.711  1.00 27.38 ? 1114 HOH A O     1 
HETATM 4234 O O     . HOH I 7 .   ? -13.561 -27.652 16.121  1.00 31.67 ? 1115 HOH A O     1 
HETATM 4235 O O     . HOH I 7 .   ? -21.901 -29.147 23.857  1.00 32.03 ? 1116 HOH A O     1 
HETATM 4236 O O     . HOH I 7 .   ? -6.302  11.738  31.903  1.00 48.47 ? 1117 HOH A O     1 
HETATM 4237 O O     . HOH I 7 .   ? -44.556 -12.138 5.393   1.00 31.56 ? 1118 HOH A O     1 
HETATM 4238 O O     . HOH I 7 .   ? -18.522 14.463  20.732  1.00 36.13 ? 1119 HOH A O     1 
HETATM 4239 O O     . HOH I 7 .   ? -20.573 -29.360 18.052  1.00 39.24 ? 1120 HOH A O     1 
HETATM 4240 O O     . HOH I 7 .   ? -24.996 2.072   25.044  1.00 34.41 ? 1121 HOH A O     1 
HETATM 4241 O O     . HOH I 7 .   ? -33.341 -42.901 29.088  1.00 36.33 ? 1122 HOH A O     1 
HETATM 4242 O O     . HOH I 7 .   ? -41.993 -33.536 31.471  1.00 45.82 ? 1123 HOH A O     1 
HETATM 4243 O O     . HOH I 7 .   ? -15.485 11.633  7.404   1.00 34.15 ? 1124 HOH A O     1 
HETATM 4244 O O     . HOH I 7 .   ? -49.735 -41.459 19.093  1.00 24.77 ? 1125 HOH A O     1 
HETATM 4245 O O     . HOH I 7 .   ? -3.423  -14.582 -5.116  1.00 28.28 ? 1126 HOH A O     1 
HETATM 4246 O O     . HOH I 7 .   ? -43.802 2.782   8.078   1.00 55.01 ? 1127 HOH A O     1 
HETATM 4247 O O     . HOH I 7 .   ? -31.160 -14.898 32.808  1.00 44.12 ? 1128 HOH A O     1 
HETATM 4248 O O     . HOH I 7 .   ? -4.510  -7.791  36.642  1.00 25.42 ? 1129 HOH A O     1 
HETATM 4249 O O     . HOH I 7 .   ? -31.483 1.979   6.970   1.00 39.66 ? 1130 HOH A O     1 
HETATM 4250 O O     . HOH I 7 .   ? -47.021 -11.670 22.144  1.00 36.51 ? 1131 HOH A O     1 
HETATM 4251 O O     . HOH I 7 .   ? -8.583  14.195  24.652  1.00 23.67 ? 1132 HOH A O     1 
HETATM 4252 O O     . HOH I 7 .   ? -52.880 -11.367 17.262  1.00 44.65 ? 1133 HOH A O     1 
HETATM 4253 O O     . HOH I 7 .   ? -15.809 -24.851 32.492  1.00 38.46 ? 1134 HOH A O     1 
HETATM 4254 O O     . HOH I 7 .   ? -25.920 10.578  18.358  1.00 41.86 ? 1135 HOH A O     1 
HETATM 4255 O O     . HOH I 7 .   ? -13.709 -16.980 18.821  1.00 46.57 ? 1136 HOH A O     1 
HETATM 4256 O O     . HOH I 7 .   ? -41.708 -25.995 31.834  1.00 17.76 ? 1137 HOH A O     1 
HETATM 4257 O O     . HOH I 7 .   ? 3.312   3.150   22.875  1.00 39.38 ? 1138 HOH A O     1 
HETATM 4258 O O     . HOH I 7 .   ? -24.325 -18.707 -11.905 1.00 45.07 ? 1139 HOH A O     1 
HETATM 4259 O O     . HOH I 7 .   ? -32.557 -31.870 34.356  0.50 16.09 ? 1140 HOH A O     1 
HETATM 4260 O O     . HOH I 7 .   ? -20.213 7.437   29.934  1.00 35.71 ? 1141 HOH A O     1 
HETATM 4261 O O     . HOH I 7 .   ? -27.645 -8.381  35.203  1.00 31.28 ? 1142 HOH A O     1 
HETATM 4262 O O     . HOH I 7 .   ? 9.777   1.795   20.575  1.00 48.67 ? 1143 HOH A O     1 
HETATM 4263 O O     . HOH I 7 .   ? -22.900 -8.595  -1.683  1.00 32.95 ? 1144 HOH A O     1 
HETATM 4264 O O     . HOH I 7 .   ? -15.116 -29.102 14.721  1.00 34.83 ? 1145 HOH A O     1 
HETATM 4265 O O     . HOH I 7 .   ? -24.941 -7.622  44.407  1.00 29.82 ? 1146 HOH A O     1 
HETATM 4266 O O     . HOH I 7 .   ? -19.887 -27.082 38.527  1.00 40.08 ? 1147 HOH A O     1 
HETATM 4267 O O     . HOH I 7 .   ? -5.251  -14.317 28.720  1.00 32.82 ? 1148 HOH A O     1 
HETATM 4268 O O     . HOH I 7 .   ? -51.740 -22.791 14.097  1.00 23.36 ? 1149 HOH A O     1 
HETATM 4269 O O     . HOH I 7 .   ? -47.734 -30.261 28.546  1.00 51.99 ? 1150 HOH A O     1 
HETATM 4270 O O     . HOH I 7 .   ? -9.295  12.685  32.894  1.00 48.11 ? 1151 HOH A O     1 
HETATM 4271 O O     . HOH I 7 .   ? 4.922   -1.940  27.491  1.00 28.52 ? 1152 HOH A O     1 
HETATM 4272 O O     . HOH I 7 .   ? -45.035 -44.985 19.464  1.00 23.07 ? 1153 HOH A O     1 
HETATM 4273 O O     . HOH I 7 .   ? -49.814 -20.669 19.813  1.00 29.98 ? 1154 HOH A O     1 
HETATM 4274 O O     . HOH I 7 .   ? -5.221  -12.875 21.919  1.00 27.20 ? 1155 HOH A O     1 
HETATM 4275 O O     . HOH I 7 .   ? -44.040 -37.158 34.258  1.00 55.00 ? 1156 HOH A O     1 
HETATM 4276 O O     . HOH I 7 .   ? -30.793 1.448   23.699  1.00 32.52 ? 1157 HOH A O     1 
HETATM 4277 O O     . HOH I 7 .   ? -12.027 14.545  25.945  1.00 37.26 ? 1158 HOH A O     1 
HETATM 4278 O O     . HOH I 7 .   ? -41.700 -42.642 10.196  1.00 45.75 ? 1159 HOH A O     1 
HETATM 4279 O O     . HOH I 7 .   ? -2.077  -26.623 8.354   1.00 37.73 ? 1160 HOH A O     1 
HETATM 4280 O O     . HOH I 7 .   ? -0.000  2.068   34.356  0.50 23.95 ? 1161 HOH A O     1 
HETATM 4281 O O     . HOH I 7 .   ? -53.961 -18.300 8.779   1.00 37.71 ? 1162 HOH A O     1 
HETATM 4282 O O     . HOH I 7 .   ? -50.068 -36.836 16.231  1.00 40.50 ? 1163 HOH A O     1 
HETATM 4283 O O     . HOH I 7 .   ? -13.220 -27.364 27.469  1.00 53.59 ? 1164 HOH A O     1 
HETATM 4284 O O     . HOH I 7 .   ? -15.248 -13.322 21.541  1.00 24.02 ? 1165 HOH A O     1 
HETATM 4285 O O     . HOH I 7 .   ? -14.250 13.449  21.807  1.00 30.77 ? 1166 HOH A O     1 
HETATM 4286 O O     . HOH I 7 .   ? -33.123 -44.227 33.410  1.00 37.02 ? 1167 HOH A O     1 
HETATM 4287 O O     . HOH I 7 .   ? -19.454 -31.933 11.445  1.00 28.17 ? 1168 HOH A O     1 
HETATM 4288 O O     . HOH I 7 .   ? -19.107 -30.287 16.081  1.00 37.13 ? 1169 HOH A O     1 
HETATM 4289 O O     . HOH I 7 .   ? -3.465  -25.703 13.224  1.00 42.07 ? 1170 HOH A O     1 
HETATM 4290 O O     . HOH I 7 .   ? -51.520 -17.779 12.349  1.00 32.13 ? 1171 HOH A O     1 
HETATM 4291 O O     . HOH I 7 .   ? -51.741 -34.996 16.756  1.00 41.75 ? 1172 HOH A O     1 
HETATM 4292 O O     . HOH I 7 .   ? -53.413 -21.858 12.206  1.00 34.38 ? 1173 HOH A O     1 
HETATM 4293 O O     . HOH I 7 .   ? -22.174 -5.465  44.928  1.00 46.53 ? 1174 HOH A O     1 
HETATM 4294 O O     . HOH I 7 .   ? -43.138 -35.789 29.730  1.00 44.26 ? 1175 HOH A O     1 
HETATM 4295 O O     . HOH I 7 .   ? -7.598  -14.365 22.921  1.00 27.84 ? 1176 HOH A O     1 
HETATM 4296 O O     . HOH I 7 .   ? -24.136 8.254   15.399  1.00 25.93 ? 1177 HOH A O     1 
HETATM 4297 O O     . HOH I 7 .   ? -40.986 -41.137 24.223  1.00 29.51 ? 1178 HOH A O     1 
HETATM 4298 O O     . HOH I 7 .   ? -25.305 -29.430 35.361  1.00 25.88 ? 1179 HOH A O     1 
HETATM 4299 O O     . HOH I 7 .   ? -30.023 3.660   21.102  1.00 39.51 ? 1180 HOH A O     1 
HETATM 4300 O O     . HOH I 7 .   ? 3.917   -13.251 30.662  1.00 32.59 ? 1181 HOH A O     1 
HETATM 4301 O O     . HOH I 7 .   ? -41.912 -31.359 32.309  1.00 30.00 ? 1182 HOH A O     1 
HETATM 4302 O O     . HOH I 7 .   ? -25.464 -36.823 24.538  1.00 32.76 ? 1183 HOH A O     1 
HETATM 4303 O O     . HOH I 7 .   ? -17.907 -29.301 25.996  1.00 43.71 ? 1184 HOH A O     1 
HETATM 4304 O O     . HOH I 7 .   ? -14.698 -1.913  39.830  1.00 49.16 ? 1185 HOH A O     1 
HETATM 4305 O O     . HOH I 7 .   ? -5.865  -13.620 19.324  1.00 36.69 ? 1186 HOH A O     1 
HETATM 4306 O O     . HOH I 7 .   ? -22.875 -27.902 32.305  1.00 41.78 ? 1187 HOH A O     1 
HETATM 4307 O O     . HOH I 7 .   ? -21.693 -33.923 26.337  1.00 41.56 ? 1188 HOH A O     1 
HETATM 4308 O O     . HOH I 7 .   ? -8.424  -14.457 20.290  1.00 31.50 ? 1189 HOH A O     1 
HETATM 4309 O O     . HOH I 7 .   ? -46.948 -13.311 5.112   1.00 28.80 ? 1190 HOH A O     1 
HETATM 4310 O O     . HOH I 7 .   ? -46.562 -7.781  -0.455  1.00 45.44 ? 1191 HOH A O     1 
HETATM 4311 O O     . HOH I 7 .   ? -10.555 -29.445 11.730  1.00 40.84 ? 1192 HOH A O     1 
HETATM 4312 O O     . HOH I 7 .   ? -23.388 -38.412 13.541  1.00 44.68 ? 1193 HOH A O     1 
HETATM 4313 O O     . HOH I 7 .   ? -12.886 -26.747 32.900  1.00 43.91 ? 1194 HOH A O     1 
HETATM 4314 O O     . HOH I 7 .   ? -8.036  -30.404 9.526   1.00 38.86 ? 1195 HOH A O     1 
HETATM 4315 O O     . HOH I 7 .   ? -19.558 -41.254 24.052  1.00 53.54 ? 1196 HOH A O     1 
HETATM 4316 O O     . HOH I 7 .   ? -5.661  -28.781 15.328  1.00 40.23 ? 1197 HOH A O     1 
HETATM 4317 O O     . HOH I 7 .   ? -53.516 -17.221 6.011   1.00 32.55 ? 1198 HOH A O     1 
HETATM 4318 O O     . HOH I 7 .   ? -26.937 -38.039 22.264  1.00 38.71 ? 1199 HOH A O     1 
HETATM 4319 O O     . HOH I 7 .   ? -55.693 -33.686 22.983  1.00 46.73 ? 1200 HOH A O     1 
HETATM 4320 O O     . HOH I 7 .   ? -51.377 -18.326 2.229   1.00 45.31 ? 1202 HOH A O     1 
HETATM 4321 O O     . HOH I 7 .   ? -46.738 -9.435  -4.014  1.00 47.10 ? 1204 HOH A O     1 
HETATM 4322 O O     . HOH I 7 .   ? -21.440 -39.930 16.156  1.00 46.32 ? 1205 HOH A O     1 
HETATM 4323 O O     . HOH I 7 .   ? -21.206 -39.164 18.610  1.00 62.27 ? 1206 HOH A O     1 
# 
